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(1R)-1-(2-naphthyl)ethylamine + H2O + O2
1-(naphthalen-2-yl)ethan-1-one + NH3 + H2O2
substrate of mutant Y228L/F242I/R283G
-
-
?
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
(1R)-1-phenylpropan-1-amine + H2O + O2
1-phenylpropan-1-one + NH3 + H2O2
mutant Y228L/R283G, 109% of the activity with (1R)-1-phenylethan-1-amine
-
-
?
(R)-alpha-methylbenzylamine + H2O + O2
alpha-methylbenzaldehyde + NH3 + H2O2
substrate of mutant Y228L/R283G, the neutral amine is the substrate
-
-
?
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine + H2O + O2
(4-chlorophenyl)(phenyl)methanone + NH3 + H2O2
no substrate of wild-type
-
-
?
1,1-diphenylmethanamine + H2O + O2
diphenylmethanone + NH3 + H2O2
no substrate of wild-type
-
-
?
1-(4-fluorophenyl)ethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
mutant Y228L/R283G, 22.7% of the activity with (1R)-1-phenylethan-1-amine
-
-
?
3,4-dihydroxy-D-phenylalanine + H2O + O2
3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
-
-
-
?
4-fluoro-D-Phe + H2O + O2
4-fluorophenylpyruvate + NH3 + H2O2
82% activity compared to D-Met
-
-
?
4-fluoro-DL-phenylalanine + H2O + O2
4-fluoro-phenylpyruvate + NH3 + H2O2
81% activity compared to D-methionine
-
-
?
a D-amino acid + H2O + O2
a 2-oxo acid + NH3 + H2O2
alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
cephalosporin C
alpha-ketoadipinyl-7-aminocephalosporanic acid
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
cephalosporin C + H2O + O2
7-aminocephalosporanic acid + ? + H2O2
conversion of cephalosporin C to 7-aminocephalosporanic acid and spontaneous decarboxylation of oxoadipyl-7-amino cephalosporanic acid is promoted by the H2O2 formed in the oxidase reaction of TvDAO
-
-
?
D-1-naphthyl-alanine + H2O + O2
?
-
-
-
?
D-1-naphthyl-glycine + H2O + O2
?
-
-
-
?
D-2-aminobutyrate + H2O + O2
2-oxobutyrate + NH3 + H2O2
-
-
-
-
?
D-2-chloro-phenylglycine + H2O + O2
(2-chlorophenyl)acetic acid + NH3 + H2O2
-
-
-
?
D-2-fluoro-phenylglycine + H2O + O2
(2-fluorophenyl)acetic acid + NH3 + H2O2
-
-
-
?
D-2-naphthyl-alanine + H2O + O2
?
-
-
-
?
D-2-naphthyl-glycine + H2O + O2
?
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
D-4-chloro-phenylglycine + H2O + O2
(4-chlorophenyl)acetic acid + NH3 + H2O2
-
-
-
?
D-4-fluoro-phenylglycine + H2O + O2
(4-fluorophenyl)acetic acid + NH3 + H2O2
-
-
-
?
D-4-hydroxy-phenylglycine + H2O + O2
(4-hydroxyphenyl)acetic acid + NH3 + H2O2
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
D-alanine + 2,6-dichlorophenolindophenol + H2O
pyruvate + reduced 2,6-dichlorophenolindophenol + H2O2
-
-
-
-
r
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
D-alanine + oxidized methylene blue + H2O
pyruvate + reduced methylene blue + H2O2
-
-
-
-
r
D-allo-isoleucine + H2O + O2
(3R)-3-hydroxy-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-allo-isoleucine + H2O + O2
?
1.0% activity compared to D-methionine
-
-
?
D-allo-threonine + H2O + O2
? + NH3 + H2O2
-
-
-
?
D-alpha-aminoadipate + H2O + O2
2-oxoadipate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxo acid + NH3 + H2O2
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
D-amino acid + H2O + O2
a 2-oxo carboxylate + NH3 + H2O2
-
-
-
-
ir
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
D-Arg + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
D-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
D-aspartate + H2O + O2
?
-
-
-
?
D-aspartate + H2O + O2
? + NH3 + H2O2
recombinant maltose-binding protein-fusion DAAO
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
D-aspartic acid + H2O + O2
oxaloacetate + NH3 + H2O2
-
weak activity
-
-
?
D-citrulline + H2O + O2
2-oxo-5-ureidopentanoate + NH3 + H2O2
-
-
-
-
r
D-citrulline + H2O + O2
2-oxo-5-ureidopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-cycloserine + H2O + O2
? + NH3 + H2O2
-
-
-
?
D-Cys + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
-
1% of the activity with D-Met
-
-
?
D-cysteine + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
-
-
?
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvic acid + NH3 + H2O2
D-ethionine + H2O + O2
4-ethylsulfanyl-2-oxobutyric acid + NH3 + H2O2
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
D-glufosinate + H2O + O2
?
-
-
-
-
ir
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
D-glutamate + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
D-glutamic acid + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
?
D-homo-phenylalanine + H2O + O2
?
-
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
D-kynurenine + H2O + O2
kynurenate + NH3 + H2O2
-
-
-
?
D-kynurenine + H2O + O2
kynurenic acid + NH3 + H2O2
-
-
-
-
?
D-kynurenine + NH3 + H2O2
kynurenic acid + NH3 + H2O2
-
-
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
D-Leu + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
D-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
D-Lys + H2O + O2
? + NH3 + H2O2
-
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
D-Met + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
best substrate
-
-
?
D-methionine + 2,6-dichloroindophenol
4-methylsulfanyl-2-oxobutanoate + reduced 2,6-dichloroindophenol
D-methionine + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
D-methionine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
-
?
D-methionine + H2O + 2,6-dichloroindophenol
?
-
-
-
-
?
D-methionine + H2O + O2
2-oxo-4-methylthiobutyric acid + NH3 + H2O2
-
-
-
-
ir
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
D-methionine + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
highly active
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
D-naphthylalanine + H2O + O2
naphthylpyruvate + NH3 + H2O2
-
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
D-Orn + H2O + O2
5-amino-2-oxopentanoate + NH3 + H2O2
34% activity compared to D-Met
-
-
?
D-ornithine + H2O + O2
5-amino-2-oxopentanoate + NH3 + H2O2
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
D-phenylalanine + H2O + O2
?
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
D-phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
D-Pro + H2O + O2
2-oxopentanoate + NH3 + H2O2
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
D-Ser + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropanoate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
D-serine + H2O + O2
?
-
-
-
?
D-serine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-Thr + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
D-Trp + H2O + O2
indole-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
D-tyrosine + H2O + O2
3-(4-hydroxyphenyl)pyruvate + NH3 + H2O2
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
D-Val + H2O + O2
2-oxoisovalerate + NH3 + H2O2
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
D-valine + H2O + O2
2-oxoisovalerate + NH3 + H2O2
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
highly active
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
DL-2-naphthyl-alanine + H2O + O2
L-2-naphthyl-alanine + 2-naphthylpyruvic acid + NH3 + H2O2
-
-
-
-
ir
DL-homophenylalanine + H2O + O2
homophenylpyruvate + NH3 + H2O2
31% activity compared to D-methionine
-
-
?
DL-tert-leucine + H2O + O2
?
0.12% activity compared to D-methionine
-
-
?
epsilon-N-benzoyl-D-lysine + H2O + O2
6-benzylamino-2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
glycine + H2O + O2
glyoxylate + NH3 + H2O2
glyphosate + H2O + O2
?
-
-
-
-
?
L-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
low activity
-
-
?
L-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
low activity
-
-
?
L-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvate + NH3 + H2O2
-
-
-
?
L-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
low activity
-
-
?
N-acetyl-D-alanine + H2O + O2
pyruvate + aminoacetate + H2O2
-
-
-
-
?
N-methyl-D-aspartate + H2O + O2
?
wild-type enzyme shows no activity, mutant enzyme M213R is active
-
-
?
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
-
-
-
?
N-methyl-DL-Leu + H2O + O2
4-methyl-2-oxopentanoate + methylamine + H2O2
5.8% activity compared to D-Met
-
-
?
N-methyl-DL-leucine + H2O + O2
?
2.1% activity compared to D-methionine
-
-
?
O-methyl-DL-serine + H2O + O2
?
0.33% activity compared to D-methionine
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
thiazolidine-2-carboxylic acid + H2O + O2
? + NH3 + H2O2
tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
?
additional information
?
-
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
no substrate of wild-type
-
-
?
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylethan-1-one + NH3 + H2O2
no substrate of wild-type, but mutant Y228L/R283G
-
-
?
a D-amino acid + H2O + O2
a 2-oxo acid + NH3 + H2O2
-
-
-
-
?
a D-amino acid + H2O + O2
a 2-oxo acid + NH3 + H2O2
-
D-amino-acid oxidase catalyzes the oxidative deamination of D-amino acids, stereoisomers of the naturally occurring L-amino acids
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
1% of the activity with D-Met
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
1% of the activity with D-Ala
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
ir
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
2% of the activity with D-Met
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
36% activity compared to D-alanine
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
391846, 391848, 391857, 391862, 391863, 655115, 655117, 671491, 685045, 685721, 685758, 695690 -
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
13% of the activity with D-Val
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
14% activity compared to D-alanine
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
-
i.e. D-Dopa
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
-
D-Dopa undergoes unidirectional chiral inversion and further suggest that D-Dopa is first oxidatively deaminated by DAAO to its alpha-keto acid and then transaminated by dopa transaminase to L-Dopa
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
-
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
-
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
-
best substrate
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
57% of the activity with D-Met
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
best substrate
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
best substrate
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
71% of the activity with D-Met
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
104% activity compared to D-Ser
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
1.6% activity compared to D-Val
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
40% of the activity with D-Pro
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
165% activity compared to D-Ser
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
97% of the activity with D-Val
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
best substrate
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
best substrate
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
enzyme works as a metabolizing agent of exogenous and endogenous free D-Ala that is abundant in aquatic invertebrates such as crustaceans and bivalve mollusks, which are potential food sources of the fish. After oral administration of D-Ala at 0.005 mM/g body weight per day to carp for 30 days, enzyme activity increases by about 8fold, 3fold, and 1.5fold in intestine, hepatopancreas, and kidney, respectively, whereas no increase is found in brain
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
the inducible enzyme plays an important physiological role in metabolizing exogenous D-Ala that is abundant in their prey invertebrates, crustaceans, and mollusks
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
0.26% activity compared to D-methionine
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
the D-amino acid is a modulator of the N-methyl-D-aspartate receptor mediated neurotransmission
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
ir
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
100% activity
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
highly active
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
100% activity
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
5.8% activity in tadpoles compared to D-proline
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
recombinant maltose-binding protein-fusion DAAO
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxo acid + NH3 + H2O2
-
-
-
?
D-amino acid + H2O + O2
2-oxo acid + NH3 + H2O2
via formation of an imino acid
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
25% of the activity with D-Ala
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
7% of the activity with D-Ala
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
2% of the activity with D-Met
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
1.1% activity compared to D-Val
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
4% of the activity with D-Pro
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
43% of the activity with D-Val
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
76% activity compared to D-Met
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
-
r
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
80% activity compared to D-methionine
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
19% activity compared to D-alanine
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
42% activity compared to D-alanine
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
2% of the activity with D-Ala
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
3% of the activity with D-Ala
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
40% of the activity with D-Met
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
-
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
-
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
65% of the activity with D-Val
-
-
?
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
0.18% of the activity with D-Ala
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
7% of the activity with D-Met
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
5.5% activity compared to D-Ser
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
38.6% activity compared to D-Ser
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
-
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
-
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
38% activity compared to D-alanine
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
67% activity compared to D-alanine
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
3% activity compared to D-alanine
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
2% activity compared to D-alanine
-
-
?
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
-
1.0% activity in tadpoles compared to D-proline
-
-
?
D-cysteine + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-sulfanylpropionate + NH3 + H2O2
-
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
-
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
-
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
-
18% activity compared to D-alanine
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
-
9% activity compared to D-alanine
-
-
?
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-DOPA + H2O + O2
3,4-dihydroxyphenylpyruvic acid + NH3 + H2O2
the maximal velocity for oxidation of D-DOPA is much greater than for D-serine
-
-
?
D-ethionine + H2O + O2
4-ethylsulfanyl-2-oxobutyric acid + NH3 + H2O2
-
-
-
-
?
D-ethionine + H2O + O2
4-ethylsulfanyl-2-oxobutyric acid + NH3 + H2O2
-
-
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
51% of the activity with D-Met
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
5% of the activity with D-Ala
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
15% of the activity with D-Ala
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
53% of the activity with D-Met
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
1.0% activity compared to D-Val
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
1% of the activity with D-Pro
-
-
?
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
81% of the activity with D-Val
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
10% of the activity with D-Met
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
54% of the activity with D-Ala
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
4% of the activity with D-Met
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
5.1% activity compared to D-Val
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
-
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
4% of the activity with D-Pro
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
9% of the activity with D-Val
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
-
-
-
?
D-glutamate + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamate + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
3% activity compared to D-alanine
-
-
?
D-glutamate + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
9% activity compared to D-alanine
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
58% activity compared to D-alanine
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
78% activity compared to D-alanine
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
4% of the activity with D-Ala
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
14% of the activity with D-Ala
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
58% of the activity with D-Met
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
3.6% activity compared to D-Val
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
3% of the activity with D-Pro
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
88% of the activity with D-Val
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
12% activity compared to D-Met
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
5.9% activity compared to D-methionine
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
60% activity compared to D-alanine
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
69% activity compared to D-alanine
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
15% of the activity with D-Met
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
19% of the activity with D-Ala
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
56% of the activity with D-Met
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
26.7% activity compared to D-Val
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
35% of the activity with D-Pro
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
76% of the activity with D-Val
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
60% activity compared to D-alanine
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
69% activity compared to D-alanine
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
42% of the activity with D-Met
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
92% of the activity with D-Ala
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
29% of the activity with D-Ala
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
57% of the activity with D-Met
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
27.2% activity compared to D-Val
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
21% of the activity with D-Pro
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
32% of the activity with D-Val
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
26% activity compared to D-Met
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
7% of the activity with D-Ala
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
best substrate
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
12% activity compared to D-methionine
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
86% activity compared to D-alanine
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
37% activity compared to D-alanine
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
2.3% activity in tadpoles compared to D-proline
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
2.4% activity compared to D-Val
-
-
?
D-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
-
-
-
?
D-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
-
-
-
?
D-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
90% activity compared to D-Met
-
-
?
D-Lys + H2O + O2
?
-
25% of the activity with D-Ala
-
-
?
D-Lys + H2O + O2
?
-
5% of the activity with D-Met
-
-
?
D-Lys + H2O + O2
?
-
2% of the activity with D-Pro
-
-
?
D-Lys + H2O + O2
?
-
17% of the activity with D-Val
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
99% activity compared to D-methionine
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
-
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
8% activity compared to D-alanine
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
poor substrate
-
-
?
D-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
7% activity compared to D-alanine
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
best substrate
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
28% of the activity with D-Ala
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
best substrate
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
2.0% activity compared to D-Val
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
75% of the activity with D-Pro
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
78% of the ativity with D-Val
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
100% activity
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
14% of the activity with D-Ala
-
-
?
D-methionine + 2,6-dichloroindophenol
4-methylsulfanyl-2-oxobutanoate + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-methionine + 2,6-dichloroindophenol
4-methylsulfanyl-2-oxobutanoate + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
with 6-dichloroindophenol as electron acceptor
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
with 6-dichloroindophenol as electron acceptor
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
100% activity
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
113% activity compared to D-alanine
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
best substrate
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
77% activity compared to D-alanine
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
by far best substrate
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
7.6% activity in tadpoles compared to D-proline
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
best substrate
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-ornithine + H2O + O2
5-amino-2-oxopentanoate + NH3 + H2O2
15% activity compared to D-methionine
-
-
?
D-ornithine + H2O + O2
5-amino-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
50% of the activity with D-Met
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
19% of the activity with D-Ala
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
41% of the activity with D-Ala
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
79% of the activity with D-Met
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
2.1% activity compared to D-Val
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
84% of the activity with D-Pro
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
36% of the activity with D-Val
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
51% activity compared to D-Met
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
1.5% of the activity with D-Ala
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
54% activity compared to D-methionine
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
80% activity compared to D-methionine
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
conversion of D-phenylalanine to 99.0% phenylpyruvate within 100 min
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
94% activity compared to D-alanine
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
r
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
44% activity compared to D-alanine
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
second best substrate
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
activity of the DAAO after incubation in water-insoluble ionic liquids is higher than in water-soluble ones
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
activity of the DAAO after incubation in water-insoluble ionic liquids is higher than in water-soluble ones
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
?
D-phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
D-phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
best substrate, 100% activity in tadpoles and adults
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
4% of the activity with D-Met
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
41% of the activity with D-Ala
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
22% of the activity with D-Ala
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
0.25% activity compared to D-methionine
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
57% of the activity with D-Met
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
46% activity compared to D-alanine
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
best substrate
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
25% of the activity with D-Val
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
21% activity compared to D-alanine
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
1.1% activity in tadpoles compared to D-proline
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
1.4% of the activity with D-Ala
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
9% of the activity with D-Met
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
6% of the activity with D-Ala
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
18% of the activity with D-Ala
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
100% activity
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
41% of the activity with D-Met
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
1.3% activity compared to D-Val
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
100% activity
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
18% of the activity with D-Pro
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
22% of the activity with D-Val
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
32% of the activity with D-Ala
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
D-serine, an endogenous agonist of the N-methyl-D-aspartate, NMDA, receptors, is effective in the treatment of schizophrenia. However, orally administered D-serine is metabolized substantially by D-amino acid oxidase diminishing its oral bioavailability
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
metabolizaation of the N-methyl D-aspartate receptor co-agonist
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
the apoprotein form of hDAAO binds the substrate D-serine, which increases FAD binding thus increasing the amount of active holoenzyme in solution
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
low catalytic efficiency and substrate affinity on the physiological substrate D-serine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
physiological effects of D-serine, overview
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
the D-amino acid is a modulator of the N-methyl-D-aspartate receptor mediated neurotransmission
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
physiological effects of D-serine, overview
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
high doses of D-serine attenuate both amphetamine-induced psychomotor activity and dopamine release and also improve performance in novel object recognition
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
poor substrate
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
astroglial enzyme plays an important role in metabolizing a neuromodulator, D-serine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
49% activity compared to D-alanine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
23% activity compared to D-alanine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
7.6% activity in tadpoles compared to D-proline
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
-
r
D-serine + H2O + O2
3-hydroxypyruvate + NH3 + H2O2
-
-
-
-
r
D-Thr + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
11.5% activity compared to D-Val
-
-
?
D-Thr + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
-
-
-
?
D-Thr + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
2% of the activity with D-Ala
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
10% of the activity with D-Met
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
2% of the activity with D-Pro
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
poor substrate
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
4% of the activity with D-Val
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
1.2% of the activity with D-Ala
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
18% activity compared to D-alanine
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
2% activity compared to D-alanine
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
-
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
9% of the activity with D-Ala
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
14% of the activity with D-Ala
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
56% of the activity with D-Met
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
1.5% activity compared to D-Val
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
2% of the activity with D-Pro
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
38% of the activity with D-val
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
92% activity compared to D-alanine
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
129% activity compared to D-alanine
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
-
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
-
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
17.6% activity compared to D-Val
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
11.6% activity compared to D-Met
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
6% of the activity with D-Ala
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
8% of the activity with D-Ala
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
26% of the activity with D-Met
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
4% of the activity with D-Pro
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-Tyr + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
17% of the activity with D-Val
-
-
?
D-tyrosine + H2O + O2
3-(4-hydroxyphenyl)pyruvate + NH3 + H2O2
-
-
-
?
D-tyrosine + H2O + O2
3-(4-hydroxyphenyl)pyruvate + NH3 + H2O2
-
-
-
-
r
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
4.7% activity compared to D-methionine
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
18% activity compared to D-alanine
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
19% activity compared to D-alanine
-
-
?
D-Val + H2O + O2
2-oxoisovalerate + NH3 + H2O2
100% activity
-
-
?
D-Val + H2O + O2
2-oxoisovalerate + NH3 + H2O2
-
-
-
-
?
D-Val + H2O + O2
2-oxoisovalerate + NH3 + H2O2
-
-
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
41% of the activity with D-Met
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
15% of the activity with D-Ala
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
62% of the activity with D-Ala
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
95% of the activity with D-Met
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
-
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
28% of the activity with D-Pro
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
-
best substrate
-
-
?
D-Val + H2O + O2
alpha-ketoisovalerate + NH3 + H2O2
8% of the activity with D-Ala
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
0.35% activity compared to D-methionine
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
best substrate
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
60% activity compared to D-alanine
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
63% activity compared to D-alanine
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
-
2% of the activity with D-Met
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
-
15% of the activity with D-Ala
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
-
-
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
-
3% of the activity with D-Met
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
1.1% activity compared to D-Val
-
-
?
Gly + H2O + O2
acetate + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
3% activity compared to D-alanine
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
poor substrate
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
2% activity compared to D-alanine
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
thiazolidine-2-carboxylic acid + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
thiazolidine-2-carboxylic acid + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
additional information
?
-
-
DAO shows no activity with D-Asp, N-methyl-D-Asp, and D-Glu
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
additional information
?
-
no activity with glycine, D-serine, D-asparagine, D-aspartate, D-glutamate, D-threonine, D-tryptophan, and cephalosporin C
-
-
?
additional information
?
-
-
no activity with glycine, D-serine, D-asparagine, D-aspartate, D-glutamate, D-threonine, D-tryptophan, and cephalosporin C
-
-
?
additional information
?
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
-
DAAO is a catabolic flavoenzyme that catalyzes the oxidative deamination of D-amino acids to the corresponding a-keto acids, hydrogen peroxide, and ammonia. DAAO is strictly specific for D-isomers of amino acids
-
-
?
additional information
?
-
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
-
D-amino acid oxidase is a flavoenzyme that catalyzes the oxidation of D-amino acids to the corresponding imino acids and hydrogen peroxide
-
-
?
additional information
?
-
-
hDAAO exhibits optimal activity toward neutral D-amino acids and marginal activity toward basic ones, while acidic D-amino acids are not oxidized, structure-function relationship analysis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
-
-
?
additional information
?
-
DAAO interacts with its physiological partner pLG72, the interaction is not inhibited by benzoate and chlorpromazine
-
-
?
additional information
?
-
-
DAAO interacts with its physiological partner pLG72, the interaction is not inhibited by benzoate and chlorpromazine
-
-
?
additional information
?
-
comparison of the kinetics of trypsin cleavage of hDAAO in the presence of various ligands, overview
-
-
?
additional information
?
-
-
comparison of the kinetics of trypsin cleavage of hDAAO in the presence of various ligands, overview
-
-
?
additional information
?
-
DAAO is mainly active on neutral, hydrophobic and slightly polar D-amino acids and shows a preference for aromatic amino acids
-
-
-
additional information
?
-
-
DAAO is mainly active on neutral, hydrophobic and slightly polar D-amino acids and shows a preference for aromatic amino acids
-
-
-
additional information
?
-
-
the amount of the neutral D-amino acids are regulated, each D-amino acid is regulated in a different way
-
-
?
additional information
?
-
-
DAO catalyzes the oxidative degradation of most of the D-amino acids in mammals
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
additional information
?
-
no substrates: L-isoleucine, L-valine, L-methionine
-
-
-
additional information
?
-
-
no substrates: L-isoleucine, L-valine, L-methionine
-
-
-
additional information
?
-
-
D-amino acid oxidase is an enzyme catalyzing the strict stereospecificity the oxidative deamination of neutral and polar D-amino acids to alpha-keto acids, NH3 and hydrogen peroxide
-
-
?
additional information
?
-
D-amino acid oxidase is a flavoenzyme that catalyzes the oxidation of D-amino acids to the corresponding imino acids and hydrogen peroxide
-
-
?
additional information
?
-
-
the flavoenzyme catalyzes the oxidative deamination of neutral and basic D-amino acids to the corresponding 2-oxo acids and H2O2 with concomitant reduction of FAD
-
-
?
additional information
?
-
-
the enzyme interacts with the mammalian protein modulator pLG72
-
-
?
additional information
?
-
-
D-aspartate and glycine are no substrates
-
-
?
additional information
?
-
-
first enzyme involved in the catabolism of D-amino acids. The inducer D-Ala acts by increasing the rate of DAAO mRNA transcription. Ammonium sulfate appears to have a negative effect on DAAO mRNA translation and on the expression of DAAO activity. The best expression of DAAO activity is obtained by growing the cells for 12 h at 30°C in the presence of glucose and D-alanine using cell pre-cultured for 10 h on glucose and L-Ala
-
-
?
additional information
?
-
best substrate is D-valine followed by D-tryptophan, D-phenylalanine, D-alanine, and D-cysteine
-
-
?
additional information
?
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
additional information
?
-
the wild-type DAAO is mainly active on neutral D-amino acids, while basic D-amino acids are poor substrates and the acidic ones are virtually not oxidized
-
-
?
additional information
?
-
-
the wild-type DAAO is mainly active on neutral D-amino acids, while basic D-amino acids are poor substrates and the acidic ones are virtually not oxidized
-
-
?
additional information
?
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
-
-
?
additional information
?
-
specific dynamic channel for the diffusion of O2 leads from solvent to the flavin Si-side. O2 affinity, catalytic center, and substrate binding of wild-type and mutant enzymes, molecular dynamics simulations built from the three-dimensional structure, PDB ID 1c0p, in which the ligand D-Ala is replaced by imino pyruvate, overview
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
additional information
?
-
no activity with D-Pro, D-Cys, D-Asp, L-Val, L-Leu, and L-Ile
-
-
?
additional information
?
-
-
no activity with D-Pro, D-Cys, D-Asp, L-Val, L-Leu, and L-Ile
-
-
?
additional information
?
-
-
activity with D-Asp is not detectable
-
-
?
additional information
?
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
D-proline is the best substrate followed by D-methionine, D-alanine, D-norleucine, D-isoleucine, and D-phenylalanine
-
-
?
additional information
?
-
-
D-proline is the best substrate followed by D-methionine, D-alanine, D-norleucine, D-isoleucine, and D-phenylalanine
-
-
?
additional information
?
-
the enzyme exhibits very low activity towards basic amino acids, and it does not oxidize those with an acidic side chain
-
-
?
additional information
?
-
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
-
DAAO is a flavoprotein that catalyzes the dehydrogenation of different D-amino acids to their imino counterparts via a reduced flavin product complex. The reduced flavin is then reoxidized by O2 to yield H2O2, whereas the imino acid spontaneously hydrolyzes to the corresponding keto acid and NH4+. DAAO is strictly stereospecific and oxidizes a variety of D-amino acids, with a preference for those having small hydrophobic side chains, followed by those bearing polar, aromatic, and basic groups
-
-
?
additional information
?
-
-
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer
-
-
?
additional information
?
-
best substrate is by far D-methionine followed by D-phenylalanine, D-tryptophan, D-valin, and D-alanine
-
-
?
additional information
?
-
D-aspartate and D-glutamate are no substrates
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
additional information
?
-
-
nearly inactive toward D-aspartic and D-glutamic acids
-
-
?
additional information
?
-
-
the enzyme is involved in the conversion of cephalosporin C
-
-
?
additional information
?
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer. The wild-type enzyme is inactive towards D-Asp, being however very active with D-Ala
-
-
?
additional information
?
-
conversion of cephalosporine C to 7-aminocephalosporanic acid and spontaneous decarboxylation of oxoadipyl-7-amino cephalosporanic acid is promoted by the H2O2 formed in the oxidase reaction of TvDAO
-
-
?
additional information
?
-
-
conversion of cephalosporine C to 7-aminocephalosporanic acid and spontaneous decarboxylation of oxoadipyl-7-amino cephalosporanic acid is promoted by the H2O2 formed in the oxidase reaction of TvDAO
-
-
?
additional information
?
-
D-allo-isoleucine, D-valine, O-methyl-DL-serine, D-alanine, and D-proline are no substrates
-
-
?
additional information
?
-
recombinant maltose-binding protein-fusion DAAO can oxidize D-alanine and D-aspartate, but not D-leucine, D-isoleucine, and D-serine
-
-
?
additional information
?
-
-
recombinant maltose-binding protein-fusion DAAO can oxidize D-alanine and D-aspartate, but not D-leucine, D-isoleucine, and D-serine
-
-
?
additional information
?
-
no activity with D-Trp, D-Tyr, D-Cys, D-Gln, D-Lys, D-Arg, D-His and D-Asp
-
-
?
additional information
?
-
DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a D-amino acid + H2O + O2
a 2-oxo acid + NH3 + H2O2
-
D-amino-acid oxidase catalyzes the oxidative deamination of D-amino acids, stereoisomers of the naturally occurring L-amino acids
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
D-2-aminobutyrate + H2O + O2
2-oxobutyrate + NH3 + H2O2
-
-
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
?
-
D-Dopa undergoes unidirectional chiral inversion and further suggest that D-Dopa is first oxidatively deaminated by DAAO to its alpha-keto acid and then transaminated by dopa transaminase to L-Dopa
-
-
?
D-3,4-dihydroxyphenylalanine + H2O + O2
? + H2O2 + NH3
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
D-alanine + H2O + O2
pyruvate + H2O2 + NH3
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
D-alpha-aminoadipate + H2O + O2
2-oxoadipate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxo acid + NH3 + H2O2
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
D-amino acid + H2O + O2
a 2-oxo carboxylate + NH3 + H2O2
-
-
-
-
ir
D-Arg + H2O + O2
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Arg + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
D-Asn + H2O + O2
2-oxosuccinamate + NH3 + H2O2
-
-
-
-
?
D-Asp + H2O + O2
oxaloacetate + NH3 + H2O2
-
-
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
D-aspartic acid + H2O + O2
oxaloacetate + NH3 + H2O2
-
weak activity
-
-
?
D-citrulline + H2O + O2
2-oxo-5-ureidopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
D-ethionine + H2O + O2
4-ethylsulfanyl-2-oxobutyric acid + NH3 + H2O2
D-Gln + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-Glu + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamic acid + H2O + O2
alpha-ketoglutarate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
D-kynurenine + H2O + O2
kynurenic acid + NH3 + H2O2
-
-
-
-
?
D-kynurenine + NH3 + H2O2
kynurenic acid + NH3 + H2O2
-
-
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
D-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
-
-
-
-
?
D-Met + H2O + O2
4-methylthio-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
D-ornithine + H2O + O2
5-amino-2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
D-proline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
D-serine + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
D-Thr + H2O + O2
2-oxo-3-hydroxybutyrate + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
D-Trp + H2O + O2
indol-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-Trp + H2O + O2
indole-3-pyruvate + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
D-Tyr + H2O + O2
4-hydroxyphenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
D-Val + H2O + O2
2-oxoisovalerate + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
Gly + H2O + O2
acetate + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
glyphosate + H2O + O2
?
-
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
thiazolidine-2-carboxylic acid + H2O + O2
? + NH3 + H2O2
additional information
?
-
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
cephalosporin C + H2O + O2
7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
enzyme works as a metabolizing agent of exogenous and endogenous free D-Ala that is abundant in aquatic invertebrates such as crustaceans and bivalve mollusks, which are potential food sources of the fish. After oral administration of D-Ala at 0.005 mM/g body weight per day to carp for 30 days, enzyme activity increases by about 8fold, 3fold, and 1.5fold in intestine, hepatopancreas, and kidney, respectively, whereas no increase is found in brain
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
the inducible enzyme plays an important physiological role in metabolizing exogenous D-Ala that is abundant in their prey invertebrates, crustaceans, and mollusks
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
?
D-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
-
-
-
-
ir
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-arginine + H2O + O2
5-guanidino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
-
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
-
-
-
?
D-asparagine + H2O + O2
2-oxosuccinamic acid + NH3 + H2O2
-
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
-
-
-
-
?
D-cysteine + H2O + O2
2-oxo-3-thiopropionic acid + NH3 + H2O2
-
-
-
-
?
D-ethionine + H2O + O2
4-ethylsulfanyl-2-oxobutyric acid + NH3 + H2O2
-
-
-
-
?
D-ethionine + H2O + O2
4-ethylsulfanyl-2-oxobutyric acid + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-glutamine + H2O + O2
2-oxoglutaramate + NH3 + H2O2
-
-
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
-
?
D-His + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-methylthio-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
D-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-Phe + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
D-Pro + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-Ser + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
D-serine, an endogenous agonist of the N-methyl-D-aspartate, NMDA, receptors, is effective in the treatment of schizophrenia. However, orally administered D-serine is metabolized substantially by D-amino acid oxidase diminishing its oral bioavailability
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
metabolizaation of the N-methyl D-aspartate receptor co-agonist
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
the apoprotein form of hDAAO binds the substrate D-serine, which increases FAD binding thus increasing the amount of active holoenzyme in solution
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
low catalytic efficiency and substrate affinity on the physiological substrate D-serine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
physiological effects of D-serine, overview
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
physiological effects of D-serine, overview
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
high doses of D-serine attenuate both amphetamine-induced psychomotor activity and dopamine release and also improve performance in novel object recognition
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionate + NH3 + H2O2
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
astroglial enzyme plays an important role in metabolizing a neuromodulator, D-serine
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
-
-
-
?
D-threonine + H2O + O2
2-oxo-3-hydroxybutyric acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indol-3-pyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
-
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-tryptophan + H2O + O2
indole-3-pyruvic acid + NH3 + H2O2
DAAO catalyzes the production of aryl hydrocarbon receptor, AHR, agonists through the enzymatic conversion of D-tryptophan to indole-3-pyruvic acid
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-tyrosine + H2O + O2
4-hydroxyphenylpyruvic acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
alpha-ketoisovaleric acid + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
-
-
-
?
glycine + 2 H2O + O2
2 formic acid + NH3 + H2O2
-
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
phenylglycine + H2O + O2
benzoylformic acid + NH3 + H2O2
-
-
-
-
?
thiazolidine-2-carboxylic acid + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
thiazolidine-2-carboxylic acid + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
additional information
?
-
-
DAAO is a catabolic flavoenzyme that catalyzes the oxidative deamination of D-amino acids to the corresponding a-keto acids, hydrogen peroxide, and ammonia. DAAO is strictly specific for D-isomers of amino acids
-
-
?
additional information
?
-
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
DAAO interacts with its physiological partner pLG72, the interaction is not inhibited by benzoate and chlorpromazine
-
-
?
additional information
?
-
-
DAAO interacts with its physiological partner pLG72, the interaction is not inhibited by benzoate and chlorpromazine
-
-
?
additional information
?
-
-
the amount of the neutral D-amino acids are regulated, each D-amino acid is regulated in a different way
-
-
?
additional information
?
-
-
DAO catalyzes the oxidative degradation of most of the D-amino acids in mammals
-
-
?
additional information
?
-
-
D-amino acid oxidase is an enzyme catalyzing the strict stereospecificity the oxidative deamination of neutral and polar D-amino acids to alpha-keto acids, NH3 and hydrogen peroxide
-
-
?
additional information
?
-
-
the flavoenzyme catalyzes the oxidative deamination of neutral and basic D-amino acids to the corresponding 2-oxo acids and H2O2 with concomitant reduction of FAD
-
-
?
additional information
?
-
-
the enzyme interacts with the mammalian protein modulator pLG72
-
-
?
additional information
?
-
-
first enzyme involved in the catabolism of D-amino acids. The inducer D-Ala acts by increasing the rate of DAAO mRNA transcription. Ammonium sulfate appears to have a negative effect on DAAO mRNA translation and on the expression of DAAO activity. The best expression of DAAO activity is obtained by growing the cells for 12 h at 30°C in the presence of glucose and D-alanine using cell pre-cultured for 10 h on glucose and L-Ala
-
-
?
additional information
?
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the conversion of cephalosporin C
-
-
?
additional information
?
-
the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview
-
-
?
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(+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine
-
MK-801, a drastic decline in the expression of DAO mRNA is observed in most brain areas 1 h after the MK-801 administration (1.6 mg/kg)
(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone
-
i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD
([4-[(3,4-dichloro-5-methyl-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
([4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
([4-[(4,5-dichloro-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
([4-[(4-bromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
100% inhibition at 0.02 mM
-
1,3-Butadien 1-carboxylic acid
-
D-phenylglycine oxidation
1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
1,4-dihydropyrrolo[3,2-c]pyrazole-5-carboxylic acid
-
1H-indole-2-carboxylic acid
-
1H-pyrrole-2-carboxylic acid
-
2,3-dimethyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
2-(2,4-dichlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-(3,3-dimethylbutyl)-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
-
-
2-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-(hydroxymethyl)-5-((4-methoxybenzyl)oxy)-4H-pyran-4-one
-
2-aminobenzoic acid
-
about 35% inhibition at 0.2 mM
2-benzyl-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
-
-
2-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-chloro-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
2-hydroxybenzoic acid
-
D-phenylglycine oxidation
2-hydroxybutyric acid
-
D-phenylglycine oxidation
2-ketobutyric acid
-
D-phenylglycine oxidation
2-nitrobenzoic acid
-
about 23% inhibition at 0.2 mM
2-oxobutyrate
-
D-alanine oxidation
2-phenyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
2-[(3,4-dichlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[(4-chlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[(4-fluorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[(benzyloxy)methyl]-5-hydroxy-4H-pyran-4-one
-
2-[2-(1H-benzimidazol-1-yl)ethyl]-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
-
-
2-[[(1Z)-1-chloroprop-1-en-1-yl]sulfanyl]prop-2-enoic acid
-
-
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
2-[[(4-chlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
2-[[(4-fluorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
2-{[(3,4-dichlorophenyl)sulfanyl]methyl}-5-hydroxy-4H-pyran-4-one
-
-
3,3-dibromo-4-chloro-5-fluoro-2,3-dihydro-1H-pyrrolo[2,3-b]pyridine
3-(2-phenylethyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-(7-hydroxy-2-oxo-4-phenyl-2H-1-benzopyran-6-yl)propanoic acid
-
-
3-(benzylsulfanyl)-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-(hydroxymethyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-benzyl-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-Bromobenzoic acid
-
D-phenylglycine oxidation
3-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-chlorobenzoic acid
-
D-phenylglycine oxidation
3-cyano-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
3-hydroxy-1,5-naphthyridin-2(1H)-one hydrobromide
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
3-hydroxy-1,7-naphthyridin-2(1H)-one hydrobromide
3-hydroxy-1,8-naphthyridin-2(1H)-one
-
-
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
3-hydroxy-2H-1-benzopyran-2-one
3-hydroxy-4-methylquinolin-2(1H)-one
3-hydroxy-5-(2-phenylethyl)pyridin-2(1H)-one
-
-
3-hydroxy-5-methylpyridin-2(1H)-one
-
-
3-hydroxy-5-methylquinolin-2(1H)-one
3-hydroxy-6-methylquinolin-2(1H)-one
3-hydroxy-7-methylquinolin-2(1H)-one
3-hydroxy-8-methylquinolin-2(1H)-one
3-hydroxypyridin-2(1H)-one
-
-
3-hydroxyquinolin-2(1H)-one
3-hydroxyquinolin-2-(1H)-one
-
-
3-hydroxyquinoline-2-(1H)-one
-
very potent inhibitor
3-methyl-1H-pyrazole-5-carboxylic acid
-
-
3-methylbenzoic acid
-
D-phenylglycine oxidation
3-methylpyrazole-5-carboxylic acid
-
-
3-Nitrobenzoic acid
-
D-phenylglycine oxidation
3-pyridin-3-yl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
3-thiophencarboxylic acid
-
3-[(cyclohexylmethyl)sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(1,2-benzoxazol-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(2H-1,3-benzodioxol-5-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(3,4-dichlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(4-chlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(4-tert-butylphenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[(6-fluoronaphthalen-2-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[([1,1'-biphenyl]-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
3-[[([1,1'-biphenyl]-4-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
-
-
4,5-dichlorofuran-2-carboxylic acid
-
4,5-dichlorothiophene-2-carboxylic acid
-
-
4,5-dimethylthiophene-2-carboxylic acid
-
-
4,6-difluoro-1-hydroxy-1,3-dihydro-2H-benzimidazol-2-one
-
-
4,6-difluoro-1-hydroxy-1H-benzo[d]imidazol-2(3H)-one
4-(difluoromethyl)thiophene-2-carboxylic acid
-
-
4-(trifluoromethyl)-1,2-benzisoxazol-3-ol
-
-
4-Aminobenzoic acid
-
about 30% inhibition at 0.2 mM
4-bromo-3-nitrobenzoate
there are two binding pockets of DAO to its inhibitor 4-bromo-3-nitrobenzoate, one is shared with substrate D-Ser and FAD, and the other is an cleft between the subunits of a DAO dimer
-
4-chloro-5-fluoro-1H-pyrrolo[2,3-b]pyridine-2,3-dione
4-fluoro-1,2-benzisoxazol-3-ol
-
-
4-hydroxy-6-(1-phenylethyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-(2-phenylethyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-(3-phenylpropyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-(phenoxymethyl)pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-(3-methoxyphenyl)ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-(4-methoxyphenyl)ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-(7-hydroxy-2-oxo-4-phenyl-2H-1-benzopyran-6-yl)ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[2-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[3-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[4-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[7-hydroxy-4-(3-methoxyphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[7-hydroxy-4-(3-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
-
-
4-hydroxy-6-[2-[7-hydroxy-4-(4-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
-
-
4-methylthiophene-2-carboxylic acid
-
-
4-nitrobenzoic acid
-
about 18% inhibition at 0.2 mM
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-3-carboxylic acid
-
4H-furo[3,2-b]pyrrole-5-carboxylic acid
4H-pyrrolo[2,3-d][1,3]oxazole-5-carboxylic acid
-
4H-pyrrolo[2,3-d][1,3]thiazole-5-carboxylic acid
-
4H-pyrrolo[3,2-d][1,3]thiazole-5-carboxylic acid
-
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
4H-thieno[3,2-b]-pyrrole-5-carboxylic acid
-
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
5,5'-dithiobis-nitrobenzoate
-
-
5,6-dichloro-1,2-benzoxazol-3-ol
-
5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylic acid
-
5-(difluoromethyl)thiophene-2-carboxylic acid
-
-
5-(trifluoromethyl)thiophene-2-carboxylic acid
-
-
5-bromo-1,2-benzisoxazol-3-ol
-
-
5-bromothiophene-2-carboxylic acid
-
-
5-chloro-3-hydroxypyridin-2(1H)-one
-
-
5-chloro-3-hydroxyquinolin-2(1H)-one
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
5-chloro-benzo[d]isoxazol-3-ol
5-chlorothiophene-2-carboxylic acid
-
-
5-ethyl-3-hydroxyquinolin-2(1H)-one
5-fluoro-3-hydroxyquinolin-2(1H)-one
5-fluorothiophene-2-carboxylic acid
-
-
5-hydroxy-2-(2-phenylethyl)-4H-pyran-4-one
-
5-hydroxy-2-(methoxymethyl)-4H-pyran-4-one
-
5-hydroxy-2-(phenoxymethyl)-4H-pyran-4-one
-
5-hydroxy-2-[(naphthalen-1-yloxy)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(naphthalen-2-yloxy)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(phenylsulfanyl)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(pyridin-3-yloxy)methyl]-4H-pyran-4-one
-
5-hydroxy-2-[(pyrimidin-2-ylsulfanyl)methyl]-4H-pyran-4-one
-
5-hydroxy-3-(2-phenylethyl)-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-3-(3-phenylpropyl)-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-3-[(2-phenylethyl)sulfanyl]-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-3-[[(4-iodophenyl)methyl]sulfanyl]-1,2,4-triazin-6(1H)-one
-
-
5-hydroxy-4-methyl-3-[(naphthalen-1-yl)methyl]pyridine-2,6(1H,3H)-dione
-
-
5-iodo-1,2-benzisoxazol-3-ol
-
-
5-methyl-1H-pyrazole-3-carboxylic acid
-
-
5-Methylpyrazole-3-carboxylate
-
-
5-methylpyrazole-3-carboxylic acid
5-Methylthiophene-2-carboxylate
-
-
5-methylthiophene-2-carboxylic acid
-
-
5-nitro-1,2-benzisoxazol-3-ol
-
-
6-(2-cyclohexylethyl)-4-hydroxypyridazin-3(2H)-one
-
-
6-(3,3-dimethylbutyl)-4-hydroxypyridazin-3(2H)-one
-
-
6-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
6-(trifluoromethyl)-1,2-benzisoxazol-3-ol
-
-
6-chloro-1,2-benzisoxazol-3-ol
-
6-chloro-1,2-benzoxazol-3-ol
-
-
6-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
6-chloro-3-hydroxyquinolin-2(1H)-one
6-chlorobenzo(d)isoxazol-3-ol
-
-
6-chlorobenzo[d]isoxazol-3-ol
6-chlorobenzo[d]isoxazole-3-ol
-
-
6-cyclohexyl-4-hydroxypyridazin-3(2H)-one
-
-
6-ethoxy-1,2-benzisoxazol-3-ol
-
-
6-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
6-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione .
-
-
6-fluoro-1,2-benzisoxazol-3-ol
-
-
6-fluoro-3-hydroxyquinolin-2(1H)-one
6-hydroxy-2-(2-(naphthalen-1-yl)ethyl)-1,2,4-triazine-3,5-(2H,4H)-dione
-
-
6-hydroxy-2-(2-phenylethyl)-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-(3-methylbutyl)-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-(3-phenylpropyl)-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-methyl-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-phenyl-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[(naphthalen-1-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[(naphthalen-2-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[2-(1H-pyrazol-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[2-(1H-pyrrolo[2,3-b]pyridin-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-hydroxy-2-[2-(pyridin-2-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
-
-
6-methoxy-1,2-benzisoxazol-3-ol
-
-
6-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
6-methyl-1,2-benzisoxazol-3-ol
-
-
6-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
6-nitro-1,2-benzisoxazol-3-ol
-
-
6-phenethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
6-[(E)-2-(4-chlorophenyl)vinyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(2-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(3,5-difluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(3,5-dimethoxyphenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(3-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(4-chlorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-(4-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-[3,5-bis(trifluoromethyl)phenyl]ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-[4-(3-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6-[2-[4-(4-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
-
-
6H-thieno[2,3-b]pyrrole-5-carboxylic acid
-
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-(5-oxoadipoamido)cephalosporanic acid
7-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-chloro-3-hydroxyquinolin-2(1H)-one
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-ethyl-3-hydroxyquinolin-2(1H)-one
7-fluoro-1,2-benzisoxazol-3-ol
-
-
7-fluoro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-fluoro-3-hydroxyquinolin-2(1H)-one
7-fluoro-6-(trifluoromethyl)-1,2-benzisoxazol-3-ol
-
-
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-hydroxypyrido[2,3-b]pyrazin-6(5H)-one
7-methyl-1,2-benzisoxazol-3-ol
-
-
7-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-chloro-3-hydroxyquinolin-2(1H)-one
8-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-ethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-ethyl-3-hydroxyquinolin-2(1H)-one
8-fluoro-3-hydroxyquinolin-2(1H)-one
8-isopropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-phenoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
adenosine 5'-monophosphate
-
-
Benzamide
-
about 32% inhibition at 0.2 mM
benzo[d]isoxazol-3-ol
-
-
Ca2+
-
83.1% residual activity at 10 mM
creatinine
75 mM, 86% inhibition
crotonic acid
-
D-phenylglycine oxidation
D-2-Hydroxy-3-methylvalerate
-
D-alanine oxidation
D-lactate
-
slight, D-alanine oxidation
D-malate
10 mM, 13.5% inhibition
DELTA1-Piperidine 2-carboxylate
-
D-lysine oxidation
DL-2-hydroxybutyrate
-
D-alanine oxidation
DL-2-Hydroxyoctanoate
-
D-alanine oxidation
glutaryl-7-aminocephalosporanic acid
Glycyl-DL-norvaline
-
slight, D-alanine oxidation
glycyl-DL-phenylalanine
-
slight, D-alanine oxidation
Glycyl-DL-tryptophan
-
slight, D-alanine oxidation
Glycyl-DL-valine
-
slight, D-alanine oxidation
HgCl2
0.1 mM, 71% inhibition
Histidyl-histidine
-
slight, D-alanine oxidation
imidazo[1,2-a]pyridine-6-carboxylic acid
-
iodoacetate
-
81.6% residual activity at 1 mM
KCl
-
about 30% residual activity at 250 mM KCl
L-histidine
-
D-histidine oxidation
L-leucine
-
D-alanine oxidation
L-norvaline
-
D-alanine oxidation
malate
-
78.6% residual activity at 10 mM
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
Mg2+
-
84.9% residual activity at 10 mM
NaCl
-
direct inhibition by NaCl is due to FAD dissociation
nicotinic acid
-
D-phenylglycine oxidation
p-Aminosalicylic acid
-
-
p-hydroxymercuribenzoate
-
significant inhibition (6.2% residual activity at 1 mM)
PCMB
75 mM, 93% inhibition
phenylmethylsulfonyl fluoride
31.8% residual activity at 10 mM
Picolinic acid
-
D-phenylglycine oxidation
poly(methylene-co-guanidine)
-
in the presence of poly(methylene-co-guanidine) (1.8%, w/v) the enzyme activity decreases irreversibly with a half-life time of about 1.75 min at 25°C
-
pyrrole-2-carboxylate
-
-
Pyrrolidine
-
slight, D-alanine oxidation
pyruvate
-
slight, D-alanine oxidation
riboflavin 5'-monophosphate
-
-
Silver nitrate
0.1 mM, 66% inhibition
Straight-chain fatty acids
-
-
succinate
-
90.7% residual activity at 1 mM
succinate semialdehyde
-
-
Tartrate
-
79.5% residual activity at 10 mM
thiophene-2-carboxylic acid
-
trans-2-Pentenoic acid
-
D-phenylglycine oxidation
trifluoro-D-alanine
-
pseudo-substrate
[[4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl](methyl)amino]acetic acid
100% inhibition at 0.02 mM
-
1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
-
-
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
-
-
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
-
-
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
-
-
3,3-dibromo-4-chloro-5-fluoro-2,3-dihydro-1H-pyrrolo[2,3-b]pyridine
-
3,3-dibromo-4-chloro-5-fluoro-2,3-dihydro-1H-pyrrolo[2,3-b]pyridine
-
-
3-hydroxy-1,5-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,5-naphthyridin-2(1H)-one hydrobromide
-
-
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
-
-
3-hydroxy-1,7-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,7-naphthyridin-2(1H)-one hydrobromide
-
-
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
-
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
-
-
3-hydroxy-2H-1-benzopyran-2-one
-
3-hydroxy-2H-1-benzopyran-2-one
-
-
3-hydroxy-4-methylquinolin-2(1H)-one
-
3-hydroxy-4-methylquinolin-2(1H)-one
-
-
3-hydroxy-5-methylquinolin-2(1H)-one
-
3-hydroxy-5-methylquinolin-2(1H)-one
-
-
3-hydroxy-6-methylquinolin-2(1H)-one
-
3-hydroxy-6-methylquinolin-2(1H)-one
-
-
3-hydroxy-7-methylquinolin-2(1H)-one
-
3-hydroxy-7-methylquinolin-2(1H)-one
-
-
3-hydroxy-8-methylquinolin-2(1H)-one
-
3-hydroxy-8-methylquinolin-2(1H)-one
-
-
3-Hydroxybenzoic acid
-
D-phenylglycine oxidation
3-Hydroxybenzoic acid
-
about 19% inhibition at 0.2 mM
3-hydroxycoumarin
-
3-hydroxyquinolin-2(1H)-one
-
3-hydroxyquinolin-2(1H)-one
-
-
3-hydroxyquinolin-2(1H)-one
-
-
3-hydroxyquinolin-2-one
-
-
3-hydroxyquinolin-2-one
-
-
3-hydroxyquinolin-2-one
-
-
3-thiophencarboxylic acid
-
-
3-thiophencarboxylic acid
-
-
4,6-difluoro-1-hydroxy-1H-benzo[d]imidazol-2(3H)-one
-
4,6-difluoro-1-hydroxy-1H-benzo[d]imidazol-2(3H)-one
-
-
4-chloro-5-fluoro-1H-pyrrolo[2,3-b]pyridine-2,3-dione
-
4-chloro-5-fluoro-1H-pyrrolo[2,3-b]pyridine-2,3-dione
-
-
4-hydroxybenzoic acid
-
D-phenylglycine oxidation
4-hydroxybenzoic acid
-
about 15% inhibition at 0.2 mM
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
-
-
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
-
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-2-carboxylic acid
-
-
4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
4H-furo[3,2-b]pyrrole-5-carboxylic acid
-
-
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
-
i.e. compound 8, a moderately potent inhibitor of human DAAO in vitro
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
-
i.e. compound 8, a moderately potent inhibitor of rat DAAO in vitro, inhibits DAAO activity in kideny by 96% and in brain by 80% resulting in a significant elevation in both plasma and cerebrospinal fluid D-serine concentration. Compound 8 fails to significantly influence amphetamine-induced psychomotor activity, nucleus accumbens dopamine release, or a dizocilpine maleate-induced deficit in novel object recognition in rats
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
-
i.e. compound 8, very specific inhibitor of DAAO
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
-
i.e. compound 8, very specific inhibitor of DAAO. Compound 8 at 200 mg/kg body weight inhibits rat kidney and cerebellar DAAO by approximately 96% and 80%, respectively. Effects after in vivo application, overview
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
-
-
5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylic acid
-
-
5,6-dihydro-4H-cyclopenta[b]thiophene-2-carboxylic acid
-
-
5-chloro-3-hydroxyquinolin-2(1H)-one
-
5-chloro-3-hydroxyquinolin-2(1H)-one
-
-
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
-
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
-
-
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
-
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
-
-
5-chloro-benzo[d]isoxazol-3-ol
-
-
5-chloro-benzo[d]isoxazol-3-ol
-
-
5-ethyl-3-hydroxyquinolin-2(1H)-one
-
5-ethyl-3-hydroxyquinolin-2(1H)-one
-
-
5-fluoro-3-hydroxyquinolin-2(1H)-one
-
5-fluoro-3-hydroxyquinolin-2(1H)-one
-
-
5-methylpyrazole-3-carboxylic acid
AS057278, selective D-amino acid oxidase inhibitor
5-methylpyrazole-3-carboxylic acid
-
i.e. AS057278
5-methylpyrazole-3-carboxylic acid
-
-
5-methylpyrazole-3-carboxylic acid
-
AS057278, selective D-amino acid oxidase inhibitor, 10 mg/kg
5-methylpyrazole-3-carboxylic acid
-
i.e. AS057278
6-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-chloro-3-hydroxyquinolin-2(1H)-one
-
6-chloro-3-hydroxyquinolin-2(1H)-one
-
-
6-chlorobenzo[d]isoxazol-3-ol
-
competitive
6-chlorobenzo[d]isoxazol-3-ol
-
-
6-chlorobenzo[d]isoxazol-3-ol
-
6-chlorobenzo[d]isoxazol-3-ol
-
-
6-chlorobenzo[d]isoxazol-3-ol
a decrease in protein fluorescence is observed at increasing 6-chlorobenzo[d]isoxazol-3-ol concentrations
6-chlorobenzo[d]isoxazol-3-ol
-
potent, competitive inhibitor
6-chlorobenzo[d]isoxazol-3-ol
-
competitive
6-chlorobenzo[d]isoxazol-3-ol
-
-
6-chlorobenzo[d]isoxazol-3-ol
-
-
6-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-fluoro-3-hydroxyquinolin-2(1H)-one
-
6-fluoro-3-hydroxyquinolin-2(1H)-one
-
-
6-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-phenethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-phenethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
6-phenethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-(5-oxoadipoamido)cephalosporanic acid
-
product inhibition
7-(5-oxoadipoamido)cephalosporanic acid
-
product inhibition
7-(5-oxoadipoamido)cephalosporanic acid
-
product inhibition
7-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-3-hydroxyquinolin-2(1H)-one
-
7-chloro-3-hydroxyquinolin-2(1H)-one
-
-
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-ethyl-3-hydroxyquinolin-2(1H)-one
-
7-ethyl-3-hydroxyquinolin-2(1H)-one
-
-
7-fluoro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-fluoro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-fluoro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-fluoro-3-hydroxyquinolin-2(1H)-one
-
7-fluoro-3-hydroxyquinolin-2(1H)-one
-
-
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-hydroxypyrido[2,3-b]pyrazin-6(5H)-one
-
7-hydroxypyrido[2,3-b]pyrazin-6(5H)-one
-
-
7-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
potent inhibitor
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
potent inhibitor
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
potent inhibitor
8-chloro-3-hydroxyquinolin-2(1H)-one
-
8-chloro-3-hydroxyquinolin-2(1H)-one
-
-
8-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-ethyl-3-hydroxyquinolin-2(1H)-one
-
8-ethyl-3-hydroxyquinolin-2(1H)-one
-
-
8-fluoro-3-hydroxyquinolin-2(1H)-one
-
8-fluoro-3-hydroxyquinolin-2(1H)-one
-
-
8-isopropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-isopropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-isopropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
-
-
aniline
-
slight, D-alanine oxidation
anthranilate
-
-
anthranilate
83.3% residual activity at 10 mM
benzoate
75 mM, 76% inhibition
benzoate
-
potent competitive inhibitor
benzoate
a classical substrate-competitive inhibitor, effect of benzoate on the FAD-binding process to hDAAO apoprotein
benzoate
-
competitive inhibitor
benzoate
a decrease in protein fluorescence is observed at increasing concentrations, with a biphasic change
benzoate
-
potent competitive inhibitor
benzoate
37% residual activity at 10 mM
benzoate
-
moderate inhibition (49.7% residual activity at 1 mM)
benzoic acid
-
-
benzoic acid
-
D-phenylglycine oxidation
benzoic acid
-
about 80% inhibition at 0.2 mM
benzoic acid
-
competitive inhibitor
beta-naphthoflavone
-
-
chlorpromazine
-
chlorpromazine
competitive versus cofactor FAD
chlorpromazine
-
a non-specific DAO inhibitor
chlorpromazine
-
FAD-competitive inhibitor
crotonate
-
-
crotonate
89.2% residual activity at 10 mM
D-serine
-
-
glutaryl-7-aminocephalosporanic acid
-
noncompetitive
glutaryl-7-aminocephalosporanic acid
-
-
glutaryl-7-aminocephalosporanic acid
-
noncompetitive
glutaryl-7-aminocephalosporanic acid
-
H2O2
-
product inhibition, competitive versus cephalosporin
H2O2
-
product inhibition, noncompetitive versus cephalosporin
H2O2
-
product inhibition, competitive versus cephalosporin
Hg2+
-
-
imidazo[1,2-a]pyridine-6-carboxylic acid
-
-
imidazo[1,2-a]pyridine-6-carboxylic acid
-
-
iodoacetamide
-
89.8% residual activity at 1 mM
kojic acid
-
kojic acid
-
D-phenylglycine oxidation
L-methionine
slightly inhibited in the presence of L-methionine
L-methionine
-
D-alanine oxidation
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
-
-
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
-
-
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
moderate inhibition (61.2% residual activity at 1 mM)
p-chloromercuribenzoate
-
0.1 mM
pLG72
-
acts as a negative effector of DAAO
-
pLG72
-
activity decreases in the presence of pLG72 (0.27 mg/ml)
-
quinoxaline-2,3-dione
-
-
quinoxaline-2,3-dione
-
-
quinoxaline-2,3-dione
-
-
risperidone
-
-
Sodium benzoate
-
inhibits the enzyme activity by by impeding the interaction of the enzyme with the flavin prosthetic group
Sodium benzoate
-
competitive inhibitor, inhibits the development of mechanical allodynia, caused by enhanced enzyme expression, in the spinal cord, overview
Sodium benzoate
inhibits the enzyme activity by impeding the interaction of the enzyme with the flavin prosthetic group
Zn2+
-
-
Zn2+
-
44% residual activity at 10 mM
additional information
benzoate and CPZ similarly modify the short-term cellular D-serine concentration but affect the cellular concentration of hDAAO differently
-
additional information
-
benzoate and CPZ similarly modify the short-term cellular D-serine concentration but affect the cellular concentration of hDAAO differently
-
additional information
identification of inhibitors by a structure based virtual screening campaign based on the X-ray structures of DAAO complexes where larger ligands shift the loop (lid opening) covering the native binding site followed by the in vitro test. Compounds bind to the active site with a salt-bridge. Displacement of and interaction with the loop covering the active site contributes significantly to the activity of the most potent compounds
-
additional information
not inhibitory: N-acetyl-cysteine at 10 mM. No change in protein fluorescence is observed with glycine (up to 50mM), ATP (up to 20mM), NMDA (up to 50mM), or D-glutamate (up to 50mM)
-
additional information
-
not inhibitory: N-acetyl-cysteine at 10 mM. No change in protein fluorescence is observed with glycine (up to 50mM), ATP (up to 20mM), NMDA (up to 50mM), or D-glutamate (up to 50mM)
-
additional information
synthesis of inhibitors that interact with loop 218-224 at the top of the binding pocket and open the lid over the active site of DAAO. The DAAO inhibitors show low nanomolar activity and low sensitivity to the substituents investigated. The interactions of the linker connecting the pendant aromatic moiety and the acidic headgroup with the enzyme are crucial for achieving significant inhibitory activity
-
additional information
-
not inhibited by sodium azide (0.8 M, 30 min)
-
additional information
-
negligible DAAO inhibition with muscimol, (S)-AMPA, 6-chloro-3-methoxybenzo[d]isoxazole, and 4,5,6,7-tetrahydrobenzo[d]isoxazol-3-ol
-
additional information
not inhibited by diethyl pyrocarbonate, malonate, and meso-tartrate
-
additional information
-
not inhibited by diethyl pyrocarbonate, malonate, and meso-tartrate
-
additional information
-
bovine serum albumin does not affect DAAO activity
-
additional information
-
resistant to the oxidants O2 and H2O2
-
additional information
-
oxidative modification of Trigonopsis variabilis D-amino acid oxidase in vivo is traceable as the conversion of Cys108 into a stable cysteine sulfinic acid, causes substantial loss of activity and thermostability of the enzyme
-
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6.25 - 7.95
(1R)-1-phenylethan-1-amine
2.9
(R)-alpha-methylbenzylamine
mutant Y228L/R283G, pH 8, 25°C. The kcat/Km profile exhibits a maximum at pH 10
2.94 - 3.73
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
-
2.4 - 5.23
1,1-diphenylmethanamine
-
0.015
2,6-dichlorophenolindophenol
-
with D-alanine
0.83 - 28
cephalosporin C
0.03 - 0.04
D-1-naphthyl-alanine
0.05 - 0.33
D-1-naphthyl-glycine
0.46
D-2-aminobutyrate
-
-
0.13 - 0.4
D-2-chloro-phenylglycine
0.5
D-2-fluoro-phenylglycine
0.04 - 0.06
D-2-naphthyl-alanine
0.01 - 0.03
D-2-naphthyl-glycine
0.03 - 0.2
D-4-chloro-phenylglycine
0.6 - 0.7
D-4-fluoro-phenylglycine
1.6 - 2.1
D-4-hydroxy-phenylglycine
83.5
D-cycloserine
pH 8.5, 25°C
2.89
D-His
-
pH 8.3, 37°C, recombinant DAO
0.15 - 0.3
D-homo-phenylalanine
0.7
D-kynurenine
pH 8.5, 25°C
0.06 - 55.9
D-phenylalanine
180
glycine
-
at pH 7.0 and 25°C
45
L-Asp
-
at pH 8.0 and 37°C
0.067
methylene blue
-
with D-alanine
18
N-Methyl-D-aspartate
pH 8.5, 25°C, mutant enzyme M213R
1.99
thiazolidine-2-carboxylate
-
-
additional information
additional information
-
6.25
(1R)-1-phenylethan-1-amine
mutant I230F/R283G, 30°C, pH 8.0
6.9
(1R)-1-phenylethan-1-amine
mutant I230C/R283G, 30°C, pH 8.0
6.98
(1R)-1-phenylethan-1-amine
mutant R283G, 30°C, pH 8.0
7.28
(1R)-1-phenylethan-1-amine
mutant I230A/R283G, 30°C, pH 8.0
7.95
(1R)-1-phenylethan-1-amine
mutant Y228L/R283G, 30°C, pH 8.0
2.94
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
2.96
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
3.73
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
2.4
1,1-diphenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
2.63
1,1-diphenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
5.23
1,1-diphenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
0.83
cephalosporin C
-
-
0.9
cephalosporin C
recombinant mutant F54S, pH 7.5, 22°C
1
cephalosporin C
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1
cephalosporin C
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1.2
cephalosporin C
recombinant mutant F54A, pH 7.5, 22°C
1.6
cephalosporin C
recombinant wild-type enzyme, pH 7.5, 22°C
1.7
cephalosporin C
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1.9
cephalosporin C
pH 8.5, 25°C, mutant enzyme Y238F
1.9
cephalosporin C
pH 8.5, 25°C, mutant enzyme Y238S
1.9
cephalosporin C
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1.9
cephalosporin C
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2.3
cephalosporin C
-
pH 8.5, 25°C
2.4
cephalosporin C
-
pH 8.5, 25°C
2.5
cephalosporin C
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2.8
cephalosporin C
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
3.8
cephalosporin C
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
4
cephalosporin C
-
pH 8.5, 25°C
4.3
cephalosporin C
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
4.8
cephalosporin C
recombinant mutant F54Y, pH 7.5, 22°C
5
cephalosporin C
pH 8.5, 25°C, wild-type enzyme
5
cephalosporin C
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
5
cephalosporin C
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
6
cephalosporin C
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
6
cephalosporin C
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
6
cephalosporin C
-
native enzyme, at 37°C
8.7
cephalosporin C
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
9
cephalosporin C
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
9
cephalosporin C
-
native enzyme, at 37°C
13
cephalosporin C
-
double fusion enzyme, at 37°C
13
cephalosporin C
mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
20
cephalosporin C
-
double fusion enzyme, at 37°C
28
cephalosporin C
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.03
D-1-naphthyl-alanine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.04
D-1-naphthyl-alanine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.05
D-1-naphthyl-glycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.33
D-1-naphthyl-glycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.13
D-2-chloro-phenylglycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.4
D-2-chloro-phenylglycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.5
D-2-fluoro-phenylglycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.5
D-2-fluoro-phenylglycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.04
D-2-naphthyl-alanine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.06
D-2-naphthyl-alanine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.01
D-2-naphthyl-glycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.03
D-2-naphthyl-glycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.03
D-4-chloro-phenylglycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.2
D-4-chloro-phenylglycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.6
D-4-fluoro-phenylglycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.7
D-4-fluoro-phenylglycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
1.6
D-4-hydroxy-phenylglycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
2.1
D-4-hydroxy-phenylglycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.23
D-Ala
pH 8.0, 37°C
0.77
D-Ala
-
wild-type enzyme
0.8
D-Ala
pH 8.5, 25°C, wild-type enzyme
0.8
D-Ala
-
pH 8.5, 25°C, wild-type enzyme, at
1.1
D-Ala
-
pH 8.5, 25°C, mutant enzyme S335G
1.2
D-Ala
-
pH 8.3, 37°C, mutant enzyme F42C
1.5
D-Ala
pH 7.5, 25°C, mutant enzyme DELTASer308-Lys321
2.5
D-Ala
-
pH 8.3, 37°C, wild-type enzyme
2.6
D-Ala
pH 8.5, 25°C, wild-type enzyme
6.89
D-Ala
-
pH 8.3, 37°C, recombinant DAO
7.5
D-Ala
pH 8.5, 25°C, mutant enzyme Y238F
7.8
D-Ala
pH 8.5, 25°C, mutant enzyme Y238S
16.7
D-Ala
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
17.8
D-Ala
pH 8.5, 25°C, mutant enzyme M213R
30.5
D-Ala
-
at pH 7.0 and 37°C
38.2
D-Ala
-
at pH 9.8 and 37°C
44
D-Ala
-
mutant enzyme E220D/Y224G
45.8
D-Ala
pH 8.5, 25°C, mutant enzyme M213R/Y238R
46
D-Ala
-
mutant enzyme R221D/Y224G
0.036
D-alanine
pH 8.5, 15°C, mutant G52V
0.2
D-alanine
apparent value, at 25°C
0.22
D-alanine
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.4
D-alanine
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.4
D-alanine
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.4
D-alanine
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.47
D-alanine
mutant P219L, pH 8.0, 25°C
0.5
D-alanine
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.6
D-alanine
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.6
D-alanine
-
mutant enzyme T60A/Q144R/K152E, apparent value, at 25°C and pH 8.5
0.7
D-alanine
free enzyme
0.7
D-alanine
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.75
D-alanine
wild-type, pH 8.0, 25°C
0.8
D-alanine
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.9
D-alanine
-
free enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C
0.9
D-alanine
-
wild type enzyme, apparent value, at 25°C and pH 8.5
1
D-alanine
immobilized enzyme
1
D-alanine
-
mutant T317A
1
D-alanine
apparent value, at 25°C
1.1
D-alanine
-
wild-type
1.1
D-alanine
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1.1
D-alanine
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1.29
D-alanine
-
38.3 kDa form
1.3
D-alanine
wild-type, pH 8.5, 25°C
1.3
D-alanine
apparent value, at 25°C
1.3
D-alanine
-
at pH 7.0 and 25°C
1.3
D-alanine
mutant enzyme Q339N, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1.3
D-alanine
pH 8, 25°C, oxygen consumption assay
1.4
D-alanine
mutant enzyme W243Y
1.4
D-alanine
mutant R120E, pH 8.5, 25°C
1.6
D-alanine
mutant enzyme W243I, assay in presence of a large excess of free FAD (0.2 mM) in assay mixture
1.6
D-alanine
-
immobilized enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C
1.7
D-alanine
apparent value, at 25°C
1.8
D-alanine
pH 8.5, 15°C, mutant Q144R
2
D-alanine
at pH 8.3 and 25°C
2
D-alanine
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
2
D-alanine
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
2
D-alanine
-
native enzyme, at 37°C
2
D-alanine
mutant R120L, pH 8.5, 25°C
2.3
D-alanine
-
wild-type
2.3
D-alanine
-
free enzyme
2.6
D-alanine
-
wild-type
2.6
D-alanine
at pH 8.3 and 25°C
2.6
D-alanine
pH 8.5, 15°C, wild-type enzyme
2.8
D-alanine
-
mutant Y224F
3
D-alanine
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
3
D-alanine
-
native enzyme, at 37°C
4
D-alanine
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
4.3
D-alanine
apparent value, at 25°C
4.5
D-alanine
at pH 8.3 and 25°C
4.63
D-alanine
-
wild-type
4.7
D-alanine
pH 8.5, 15°C, mutant S19G/S120P/Q144R/K321M/A345V
4.9
D-alanine
-
mutant enzyme M213G, apparent value, at 25°C and pH 8.5
5.5
D-alanine
apparent value, reconstituted holoenzyme at pH 8.0 and 30°C
6
D-alanine
-
double fusion enzyme, at 37°C
7
D-alanine
apparent value, at 25°C
8
D-alanine
-
mutant G281C
8.8
D-alanine
at pH 8.3 and 25°C
9.36
D-alanine
-
mutant D206E
13
D-alanine
-
FAD-S mutant enzyme
13
D-alanine
-
double fusion enzyme, at 37°C
18
D-alanine
mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
18.12
D-alanine
-
mutant D206A
18.5
D-alanine
-
mutant enzyme M213R, apparent value, at 25°C and pH 8.5
20.52
D-alanine
-
mutant D206S
27
D-alanine
-
mutant Y228F
40
D-alanine
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
140
D-alanine
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
310
D-alanine
-
mutant R285A
800
D-alanine
-
mutant R285K
1.01
D-Arg
-
pH 8.3, 37°C, recombinant DAO
3
D-Arg
-
mutant enzyme E220D/Y224G
3
D-Arg
-
mutant enzyme R221D/Y224G
13
D-Arg
-
wild-type enzyme
1.3
D-arginine
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2 - 3
D-arginine
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2.5
D-arginine
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
5.5
D-arginine
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
5.5
D-arginine
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
6.7
D-arginine
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
9.2
D-arginine
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
9.7
D-arginine
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
13
D-arginine
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
18
D-arginine
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
19.2
D-arginine
pH 8, 55°C
29
D-arginine
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
11
D-Asn
pH 8.5, 25°C, mutant enzyme M213R
14.4
D-Asn
pH 8.5, 25°C, wild-type enzyme
22
D-Asn
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
22.6
D-Asn
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
29
D-Asn
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
50
D-Asn
-
Km above 50 mM, mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
2
D-Asp
pH 8.5, 25°C, mutant enzyme M213R
18
D-Asp
-
pH 8.5, 25°C, wild-type enzyme
18
D-Asp
pH 8.5, 25°C, wild-type enzyme
28
D-Asp
pH 8.5, 25°C, mutant enzyme M213R/Y238R
30
D-Asp
-
pH 8.5, 25°C, mutant enzyme S335G
43
D-Asp
-
at pH 8.0 and 37°C
2000
D-Asp
-
pH 8.5, 25°C
2
D-Aspartate
mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
5.2
D-Aspartate
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
15
D-Aspartate
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
15
D-Aspartate
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
17
D-Aspartate
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
18
D-Aspartate
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
30
D-Aspartate
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
33
D-Aspartate
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
53
D-Aspartate
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
61
D-Aspartate
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
72
D-Aspartate
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
98
D-Aspartate
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
150
D-Aspartate
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2000
D-Aspartate
-
at pH 7.0 and 25°C
0.6
D-cysteine
pH 8.5, 25°C
7.5
D-cysteine
wild-type, pH 8.5, 25°C
17.6
D-cysteine
mutant R120E, pH 8.5, 25°C
26.7
D-cysteine
mutant R120L, pH 8.5, 25°C
1.5
D-Dopa
-
at pH 7.0 and 25°C
1.5
D-Dopa
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
3.8
D-Gln
pH 8.5, 25°C, mutant enzyme M213R
4.6
D-Gln
pH 8.5, 25°C, wild-type enzyme
33
D-Glu
pH 8.5, 25°C, mutant enzyme M213R
77.3
D-Glu
pH 8.5, 25°C, wild-type enzyme
5.1
D-glutamate
-
mutant enzyme M213G, apparent value, at 25°C and pH 8.5
12.1
D-glutamate
pH 8, 55°C
21.1
D-glutamate
-
mutant enzyme M213R, apparent value, at 25°C and pH 8.5
76
D-glutamate
-
wild type enzyme, apparent value, at 25°C and pH 8.5
76.4
D-glutamate
pH 8, 25°C, oxygen consumption assay
101
D-glutamate
-
mutant enzyme T60A/Q144R/K152E, apparent value, at 25°C and pH 8.5
2.5
D-glutamine
-
mutant enzyme M213G, apparent value, at 25°C and pH 8.5
5.4
D-glutamine
-
mutant enzyme M213R, apparent value, at 25°C and pH 8.5
5.4
D-glutamine
-
wild type enzyme, apparent value, at 25°C and pH 8.5
6
D-glutamine
-
mutant enzyme T60A/Q144R/K152E, apparent value, at 25°C and pH 8.5
0.15
D-homo-phenylalanine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.3
D-homo-phenylalanine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.052
D-Ile
at pH 8.0 and 60°C
0.049
D-Leu
at pH 8.0 and 60°C
0.227
D-Leu
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.78
D-Leu
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
1.19
D-Leu
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
1.81
D-Leu
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.08
D-leucine
-
-
0.425
D-Lys
pH 8.0, 37°C
10
D-Lys
-
wild-type enzyme
14
D-Lys
-
mutant enzyme E220D/Y224G
20
D-Lys
-
mutant enzyme R221D/Y224G
29.3
D-Lys
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
8
D-Lysine
-
mutant enzyme M213G, apparent value, at 25°C and pH 8.5
14.6
D-Lysine
-
wild type enzyme, apparent value, at 25°C and pH 8.5
14.6
D-Lysine
pH 8, 25°C, oxygen consumption assay
16.6
D-Lysine
-
mutant enzyme T60A/Q144R/K152E, apparent value, at 25°C and pH 8.5
0.2
D-Met
pH 8.5, 25°C, wild-type enzyme
0.4
D-Met
-
pH 8.3, 37°C, mutant enzyme F42C
0.46
D-Met
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.65
D-Met
-
wild-type enzyme
0.67
D-Met
-
mutant enzyme E220D/Y224G
0.67
D-Met
-
mutant enzyme R221D/Y224G
0.9
D-Met
-
pH 8.3, 37°C, wild-type enzyme
1.5
D-Met
pH 8.5, 25°C, mutant enzyme M213R
2.9
D-Met
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
2.96
D-Met
at pH 8.0 and 37°C
3.3
D-Met
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
4.2
D-Met
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.21
D-methionine
pH 8, 55°C
0.3
D-methionine
-
mutant enzyme T60A/Q144R/K152E, apparent value, at 25°C and pH 8.5
0.6
D-methionine
-
wild type enzyme, apparent value, at 25°C and pH 8.5
0.8
D-methionine
-
mutant enzyme M213G, apparent value, at 25°C and pH 8.5
1.2
D-methionine
-
mutant enzyme M213R, apparent value, at 25°C and pH 8.5
15.6
D-methionine
-
mutant Y224F
50
D-methionine
-
mutant Y228F
143
D-methionine
-
wild-type
0.39
D-norleucine
-
-
0.063
D-Norvaline
-
-
0.04
D-Phe
pH 8.5, 25°C, mutant enzyme Y238F
0.068
D-Phe
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.07
D-Phe
pH 8.5, 25°C, mutant enzyme Y238S
0.134
D-Phe
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.3
D-Phe
pH 8.5, 25°C, wild-type enzyme
0.37
D-Phe
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.77
D-Phe
-
mutant enzyme R221D/Y224G
1.4
D-Phe
-
wild-type enzyme
1.4
D-Phe
-
mutant enzyme E220D/Y224G
1.68
D-Phe
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
1.9
D-Phe
-
pH 8.3, 37°C, mutant enzyme F42C
2.72
D-Phe
-
pH 8.3, 37°C, recombinant DAO
3.6
D-Phe
-
pH 8.3, 37°C, wild-type enzyme
0.06
D-phenylalanine
-
-
0.2
D-phenylalanine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.3
D-phenylalanine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
1.2
D-phenylalanine
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
1.38
D-phenylalanine
-
pH 8.0
1.4
D-phenylalanine
-
wild-type
2.7
D-phenylalanine
-
at pH 7.0 and 25°C
5.01
D-phenylalanine
wild-type, 30°C, pH 8.0
7.5
D-phenylalanine
-
mutant Y224F
8.41
D-phenylalanine
mutant Y228L, 30°C, pH 8.0
9.1
D-phenylalanine
-
mutant T317A
18.3
D-phenylalanine
-
mutant Y228F
35
D-phenylalanine
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
55.9
D-phenylalanine
-
wild-type
0.38
D-phenylglycine
-
-
3.5
D-phenylglycine
wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
5.2
D-phenylglycine
mutant enzyme M213G, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C
0.33
D-Pro
-
at pH 8.0 and 37°C
0.38
D-Pro
-
at pH 7.5 and 37°C
0.56
D-Pro
-
wild-type enzyme
0.85
D-Pro
-
at pH 8.5 and 37°C
4.1
D-Pro
-
mutant enzyme E220D/Y224G
7.7
D-Pro
-
mutant enzyme R221D/Y224G
12.3
D-Pro
pH 8.5, 25°C, mutant enzyme Y238S
13.5
D-Pro
pH 8.5, 25°C, mutant enzyme Y238F
21.5
D-Pro
pH 8.5, 25°C, wild-type enzyme
21.5
D-Pro
-
pH 8.5, 25°C, wild-type enzyme
1280
D-Pro
pH 8.5, 25°C, mutant enzyme M213R
0.73
D-proline
mutant P219L, pH 8.0, 25°C
1.1
D-proline
-
wild-type
1.2
D-proline
-
mutant T317A
1.23
D-proline
wild-type, pH 8.0, 25°C
5.6
D-proline
-
immobilized wild type enzyme, at 25°C
8.5
D-proline
-
at pH 7.0 and 25°C
9.1
D-proline
-
mutant Y224F
9.5
D-proline
-
wild-type
12.2
D-proline
-
mutant Y228F
12.5
D-proline
-
free wild type enzyme, at 25°C
15.5
D-proline
-
38.3 kDa form
86
D-proline
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
0.909
D-Ser
pH 8.0, 37°C
1.7
D-Ser
pH 8.5, 25°C, mutant enzyme Y238F
2.9
D-Ser
pH 8.5, 25°C, mutant enzyme Y238S
3.3
D-Ser
-
wild-type enzyme
3.62
D-Ser
-
apparent value, immobilized enzyme
4.7
D-Ser
-
pH 8.3, 37°C, mutant enzyme F42C
12.7
D-Ser
-
pH 8.3, 37°C, wild-type enzyme
13.7
D-Ser
pH 8.5, 25°C, wild-type enzyme
13.75
D-Ser
-
apparent value, free enzyme
20
D-Ser
-
pH 8.3, 37°C, recombinant DAO
36.6
D-Ser
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.6
D-serine
wild-type, pH 8.5, 25°C
0.6
D-serine
mutant R120E, pH 8.5, 25°C
0.7
D-serine
mutant R120L, pH 8.5, 25°C
1.36
D-serine
mutant P219L, pH 8.0, 25°C
3.9
D-serine
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
4
D-serine
pH 8.5, 25°C, recombinant EGFP-DAAO
4.29
D-serine
wild-type, pH 8.0, 25°C
7
D-serine
pH 8.5, 25°C, recombinant wild-type DAAO
7.5
D-serine
-
at pH 7.0 and 25°C
20.8
D-serine
-
mutant T317A
310
D-serine
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
8.16
D-Thr
at pH 8.0 and 60°C
11.1
D-Thr
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.2
D-Trp
pH 8.5, 25°C, mutant enzyme Y238S
0.3
D-Trp
pH 8.5, 25°C, mutant enzyme Y238F
0.3
D-Trp
pH 8.5, 25°C, wild-type enzyme
0.4
D-Trp
pH 7.5, 25°C, mutant enzyme DELTASer308-Lys321
0.45
D-Trp
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.46
D-Trp
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.49
D-Trp
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
2.7
D-Trp
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.17
D-tryptophan
-
-
0.7
D-tryptophan
-
immobilized enzyme
1.2
D-tryptophan
-
free enzyme
1.5
D-tryptophan
-
at pH 7.0 and 25°C
15
D-tryptophan
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
0.087
D-Tyr
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.197
D-Tyr
at pH 8.0 and 60°C
0.45
D-Tyr
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.84
D-Tyr
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
1.1
D-tyrosine
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
1.5
D-tyrosine
-
at pH 7.0 and 25°C
0.094
D-Val
at pH 8.0 and 60°C
0.63
D-Val
-
wild-type enzyme
3.1
D-Val
-
mutant enzyme E220D/Y224G
3.7
D-Val
-
mutant enzyme R221D/Y224G
6
D-Val
pH 8.5, 25°C, mutant enzyme Y238F
6.1
D-Val
pH 8.5, 25°C, mutant enzyme Y238S
14.4
D-Val
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
18.9
D-Val
pH 8.5, 25°C, wild-type enzyme
41
D-Val
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
46
D-Val
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.63
D-valine
pH 8, 55°C
0.67
D-valine
-
wild-type
1.3
D-valine
-
immobilized wild type enzyme, at 25°C
3.5
D-valine
-
free enzyme
4.3
D-valine
-
mutant T317A
18.9
D-valine
-
free wild type enzyme, at 25°C
140
Gly
-
pH 8.3, 25°C
43.11
L-Ala
-
at pH 9.8 and 37°C
362
L-Ala
-
at pH 7.0 and 37°C
20
L-Pro
-
at pH 8.0 and 37°C
252
L-Pro
-
at pH 7.5 and 37°C
1800
L-Pro
-
at pH 8.5 and 37°C
0.06
O2
-
mutant R285K
0.15
O2
at pH 8.3 and 25°C
0.15
O2
pH 8.5, 15°C, mutant G52V
0.18
O2
-
with D-methionine
0.25
O2
-
pH 8.5, 25°C, mutant enzyme S335G, reaction with D-Ala
0.26
O2
pH 8.5, 25°C, mutant enzyme Y238F
0.5
O2
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
0.8
O2
at pH 8.3 and 25°C
0.95
O2
-
cephalosporin C
0.96
O2
pH 8.5, 25°C, mutant enzyme Y238S
1.2
O2
at pH 8.3 and 25°C
1.4
O2
pH 8.5, 15°C, mutant Q144R
2.3
O2
pH 8.5, 25°C, wild-type enzyme
2.3
O2
-
pH 8.5, 25°C, wild-type enzyme, reaction with D-Ala
2.3
O2
at pH 8.3 and 25°C
3
O2
pH 8.5, 15°C, wild-type enzyme
5
O2
pH 8.5, 15°C, wild-type enzyme
5 - 20
O2
mutant Y228L/R283G, pH 8, 25°C
6.1
O2
pH 8.5, 15°C, mutant S19G/S120P/Q144R/K321M/A345V
additional information
additional information
-
the dextran-conjugated enzyme shows decreased KM-values for D-amino acids
-
additional information
additional information
steady-state kinetics, reductive and oxidative half-reactions, overview
-
additional information
additional information
DAAO-lingand interaction kinetics, overview
-
additional information
additional information
-
DAAO-lingand interaction kinetics, overview
-
additional information
additional information
-
kinetics in comparison to the human enzyme, overview
-
additional information
additional information
reaction kinetics of oxidative and reductive half-reactions of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.047 - 9.93
(1R)-1-phenylethan-1-amine
88
(R)-alpha-methylbenzylamine
mutant Y228L/R283G, pH 8, 25°C
4.33 - 6.01
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
-
0.366 - 3.42
1,1-diphenylmethanamine
-
1.3 - 4400
cephalosporin C
0.77
D-cycloserine
pH 8.5, 25°C
90.7
D-glutamate
pH 8, 55°C
1.51
D-His
-
pH 8.3, 37°C, recombinant DAO
0.09
D-kynurenine
pH 8.5, 25°C
1.72 - 55.9
D-phenylalanine
0.9
glycine
-
at pH 7.0 and 25°C
0.89
L-Asp
-
at pH 8.0 and 37°C
79
N-Methyl-D-aspartate
pH 8.5, 25°C, mutant enzyme M213R
0.047
(1R)-1-phenylethan-1-amine
mutant I230F/R283G, 30°C, pH 8.0
0.111
(1R)-1-phenylethan-1-amine
mutant I230C/R283G, 30°C, pH 8.0
0.349
(1R)-1-phenylethan-1-amine
mutant I230A/R283G, 30°C, pH 8.0
1.46
(1R)-1-phenylethan-1-amine
mutant R283G, 30°C, pH 8.0
9.93
(1R)-1-phenylethan-1-amine
mutant Y228L/R283G, 30°C, pH 8.0
4.33
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
5.48
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
6.01
(RS)-1-(4-chlorophenyl)-1-phenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
0.366
1,1-diphenylmethanamine
mutant I230F/R283G, 30°C, pH 8.0
-
3.3
1,1-diphenylmethanamine
mutant I230A/R283G, 30°C, pH 8.0
-
3.42
1,1-diphenylmethanamine
mutant I230C/R283G, 30°C, pH 8.0
-
1.3
cephalosporin C
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
3 - 6
cephalosporin C
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
3.6
cephalosporin C
mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
4.4
cephalosporin C
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
6.167
cephalosporin C
recombinant wild-type enzyme, pH 7.5, 22°C
7
cephalosporin C
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
7.3
cephalosporin C
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
7.8
cephalosporin C
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
15
cephalosporin C
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
16.67
cephalosporin C
recombinant mutant F54S, pH 7.5, 22°C
17
cephalosporin C
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
18.33
cephalosporin C
recombinant mutant F54A, pH 7.5, 22°C
24
cephalosporin C
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
24
cephalosporin C
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
26
cephalosporin C
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
36.67
cephalosporin C
recombinant mutant F54Y, pH 7.5, 22°C
39
cephalosporin C
-
pH 8.5, 25°C
50
cephalosporin C
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
55
cephalosporin C
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
55
cephalosporin C
-
native enzyme, at 37°C
57
cephalosporin C
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
64
cephalosporin C
-
double fusion enzyme, at 37°C
70
cephalosporin C
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
70
cephalosporin C
-
native enzyme, at 37°C
72
cephalosporin C
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
80
cephalosporin C
-
double fusion enzyme, at 37°C
4300
cephalosporin C
-
pH 8.5, 25°C
4400
cephalosporin C
-
pH 8.5, 25°C
0.75
D-Ala
-
mutant enzyme R221D/Y224G
3
D-Ala
-
mutant enzyme E220D/Y224G
6.5
D-Ala
-
wild-type enzyme
14.9
D-Ala
-
pH 8.3, 37°C, recombinant DAO
82
D-Ala
-
pH 8.5, 25°C, mutant enzyme S335G
108.6
D-Ala
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
120
D-Ala
pH 8.5, 25°C, mutant enzyme Y238S
125
D-Ala
pH 8.5, 25°C, mutant enzyme Y238F
133.3
D-Ala
-
at pH 9.8 and 37°C
151.2
D-Ala
-
at pH 7.0 and 37°C
278
D-Ala
pH 8.5, 25°C, mutant enzyme M213R
350
D-Ala
-
pH 8.5, 25°C, wild-type enzyme
350
D-Ala
pH 8.5, 25°C, wild-type enzyme
630
D-Ala
pH 8.5, 25°C, mutant enzyme M213R
2740
D-Ala
-
pH 8.5, 25°C
4880
D-Ala
-
pH 8.5, 25°C
5000
D-Ala
pH 8.5, 25°C, wild-type enzyme
0.000167
D-alanine
-
mutant D206A
0.001
D-alanine
-
mutant D206S
0.00233
D-alanine
-
mutant D206E
0.00567
D-alanine
-
wild-type
0.05
D-alanine
-
mutant R285A
0.33
D-alanine
pH 8.5, 15°C, mutant G52V
0.63
D-alanine
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.79
D-alanine
mutant enzyme Q339N, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.8
D-alanine
-
mutant R285K
0.92
D-alanine
-
mutant T317A
1.5
D-alanine
-
mutant G281C
2.6
D-alanine
-
FAD-S mutant enzyme
3.7
D-alanine
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
4.2
D-alanine
-
mutant Y223S
5
D-alanine
-
mutant Y228F
5.2
D-alanine
wild-type, pH 8.5, 25°C
5.2
D-alanine
apparent value, at 25°C
5.2
D-alanine
-
at pH 7.0 and 25°C
6.9
D-alanine
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
7.3
D-alanine
apparent value, at 25°C
7.33
D-alanine
-
D isotope
8.3
D-alanine
mutant P219L, pH 8.0, 25°C
8.5
D-alanine
-
wild-type
9.2
D-alanine
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
9.48
D-alanine
wild-type, pH 8.0, 25°C
10
D-alanine
at pH 8.3 and 25°C
10
D-alanine
mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
11.6
D-alanine
-
mutant Y224F
12.6
D-alanine
mutant R120E, pH 8.5, 25°C
12.7
D-alanine
-
wild-type
13.8
D-alanine
immobilized enzyme
14.7
D-alanine
at pH 8.3 and 25°C
15
D-alanine
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
17.3
D-alanine
mutant R120L, pH 8.5, 25°C
23.3
D-alanine
-
immobilized enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C
25
D-alanine
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
25
D-alanine
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
27
D-alanine
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
33.8
D-alanine
free enzyme
44
D-alanine
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
46
D-alanine
apparent value, at 25°C
48
D-alanine
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
51
D-alanine
-
immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
52.4
D-alanine
-
free enzyme, in 100 mM potassium phosphate buffer at pH 8.0 and 25°C
53
D-alanine
at pH 8.3 and 25°C
60
D-alanine
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
60
D-alanine
-
native enzyme, at 37°C
67
D-alanine
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
70.8
D-alanine
-
D isotope
74
D-alanine
-
free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C
74
D-alanine
-
native enzyme, at 37°C
75
D-alanine
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
78
D-alanine
-
double fusion enzyme, at 37°C
80
D-alanine
apparent value, at 25°C
81
D-alanine
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
85
D-alanine
apparent value, at 25°C
88
D-alanine
-
double fusion enzyme, at 37°C
95
D-alanine
apparent value, at 25°C
95
D-alanine
apparent value, reconstituted holoenzyme at pH 8.0 and 30°C
140
D-alanine
pH 8.5, 15°C, mutant Q144R
210
D-alanine
-
mutant Y223F
330
D-alanine
pH 8.5, 15°C, wild-type enzyme
350
D-alanine
-
wild-type
350
D-alanine
at pH 8.3 and 25°C
370
D-alanine
pH 8.5, 15°C, mutant S19G/S120P/Q144R/K321M/A345V
1.83
D-Arg
-
mutant enzyme I223D/Y224G
2
D-Arg
-
mutant enzymeY224G
2.83
D-Arg
-
pH 8.3, 37°C, recombinant DAO
3.5
D-Arg
-
wild-type enzyme
4
D-Arg
-
mutant enzyme E220D/Y224G
4
D-Arg
-
mutant enzyme G222D/Y224G
7.5
D-Arg
-
mutant enzyme R221D/Y224G
0.2
D-arginine
kcat less than 0.2/s, mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.43
D-arginine
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2.1
D-arginine
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2.6
D-arginine
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
3.2
D-arginine
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
3.6
D-arginine
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
6.5
D-arginine
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
7.3
D-arginine
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
8.6
D-arginine
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
11
D-arginine
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
14
D-arginine
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
20
D-arginine
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
45.6
D-arginine
pH 8, 55°C
0.7
D-Asn
-
Km less than 0.7 s-1, mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
13
D-Asn
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
50
D-Asn
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
62.4
D-Asn
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
106
D-Asn
pH 8.5, 25°C, mutant enzyme M213R
1300
D-Asn
pH 8.5, 25°C, wild-type enzyme
0.95
D-Asp
-
at pH 8.0 and 37°C
29
D-Asp
pH 8.5, 25°C, wild-type enzyme
235
D-Asp
pH 8.5, 25°C, mutant enzyme M213R
1665
D-Asp
pH 8.5, 25°C, mutant enzyme M213R/Y238R
0.09
D-Aspartate
mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.26
D-Aspartate
mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.37
D-Aspartate
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.5
D-Aspartate
mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.5
D-Aspartate
wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.56
D-Aspartate
mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.67
D-Aspartate
mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
0.9
D-Aspartate
mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
1
D-Aspartate
mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
2.5
D-Aspartate
mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
3.2
D-Aspartate
mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
3.9
D-Aspartate
mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
6
D-Aspartate
mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value
6.7
D-Aspartate
-
at pH 7.0 and 25°C
3
D-cysteine
wild-type, pH 8.5, 25°C
8.5
D-cysteine
mutant R120E, pH 8.5, 25°C
8.6
D-cysteine
pH 8.5, 25°C
11.3
D-cysteine
mutant R120L, pH 8.5, 25°C
21.67
D-Dopa
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
21.7
D-Dopa
-
at pH 7.0 and 25°C
290
D-Gln
pH 8.5, 25°C, mutant enzyme M213R
1135
D-Gln
pH 8.5, 25°C, wild-type enzyme
60
D-Glu
pH 8.5, 25°C, wild-type enzyme
975
D-Glu
pH 8.5, 25°C, mutant enzyme M213R
23
D-Ile
at pH 8.0 and 60°C
24
D-Leu
at pH 8.0 and 60°C
29.1
D-Leu
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
46
D-Leu
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
56
D-Leu
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
66.6
D-Leu
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.8
D-Lys
-
wild-type enzyme
2.33
D-Lys
-
mutant enzymeY224G
3
D-Lys
-
mutant enzyme I223D/Y224G
3.33
D-Lys
-
mutant enzyme E220D/Y224G
3.54
D-Lys
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
5
D-Lys
-
mutant enzyme G222D/Y224G
5
D-Lys
-
mutant enzyme R221D/Y224G
1.33
D-Met
-
mutant enzyme I223D/Y224G
1.38
D-Met
-
mutant enzymeY224G
2.5
D-Met
-
mutant enzyme G222D/Y224G
6.83
D-Met
-
wild-type enzyme
9
D-Met
-
mutant enzyme R221D/Y224G
10.5
D-Met
-
mutant enzyme E220D/Y224G
42
D-Met
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
63
D-Met
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
80.5
D-Met
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
89
D-Met
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
680
D-Met
pH 8.5, 25°C, mutant enzyme M213R
4600
D-Met
pH 8.5, 25°C, wild-type enzyme
0.84
D-methionine
-
recombinant mutant C108S, pH 7.5, 37°C, with 6-dichloroindophenolate
1.5
D-methionine
-
recombinant wild-type enzyme, pH 7.5, 37°C, with 6-dichloroindophenolate
2.8
D-methionine
-
recombinant mutant C108D, pH 7.5, 37°C, with 6-dichloroindophenolate
47.5
D-methionine
-
mutant Y228F
75
D-methionine
-
recombinant mutant C108D, pH 7.5, 37°C, with O2
92
D-methionine
-
mutant Y224F
110
D-methionine
-
recombinant mutant C108S, pH 7.5, 37°C, with O2
120
D-methionine
pH 8, 55°C
143
D-methionine
-
wild-type
200
D-methionine
-
recombinant wild-type enzyme, pH 7.5, 37°C, with O2
0.4
D-Phe
-
mutant enzyme E220D/Y224G
3
D-Phe
-
mutant enzyme I223D/Y224G
3.17
D-Phe
-
mutant enzymeY224G
3.5
D-Phe
-
mutant enzyme G222D/Y224G
13
D-Phe
-
mutant enzyme R221D/Y224G
16.7
D-Phe
-
wild-type enzyme
25.1
D-Phe
-
pH 8.3, 37°C, recombinant DAO
27.2
D-Phe
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
47.1
D-Phe
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
53.33
D-Phe
-
mutant enzyme E220D/Y224G
58.8
D-Phe
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
63
D-Phe
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
1.72
D-phenylalanine
mutant Y228L, 30°C, pH 8.0
2.4
D-phenylalanine
-
mutant T317A
5.19
D-phenylalanine
wild-type, 30°C, pH 8.0
6.6
D-phenylalanine
-
at pH 7.0 and 25°C
7.1
D-phenylalanine
-
mutant Y228F
8.5
D-phenylalanine
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
15.5
D-phenylalanine
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
17
D-phenylalanine
-
wild-type
48.8
D-phenylalanine
-
mutant Y224F
55.9
D-phenylalanine
-
wild-type
0.052 - 2.1
D-Pro
-
wild-type enzyme
1.67
D-Pro
-
mutant enzymeY224G
3.5
D-Pro
-
mutant enzyme G222D/Y224G
3.83
D-Pro
-
mutant enzyme R221D/Y224G
4.33
D-Pro
-
mutant enzyme E220D/Y224G
10.2
D-Pro
-
pH 8.5, 25°C
10.33
D-Pro
-
wild-type enzyme
43.3
D-Pro
-
at pH 8.5 and 37°C
50.2
D-Pro
-
at pH 7.5 and 37°C
107.3
D-Pro
-
at pH 8.0 and 37°C
1615
D-Pro
pH 8.5, 25°C, mutant enzyme M213R
4640
D-Pro
pH 8.5, 25°C, wild-type enzyme
9.7
D-proline
-
mutant T317A
10.2
D-proline
-
at pH 7.0 and 25°C
11.7
D-proline
-
mutant Y228F
26.57
D-proline
wild-type, pH 8.0, 25°C
29.53
D-proline
mutant P219L, pH 8.0, 25°C
47
D-proline
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
83.7
D-proline
-
mutant Y224F
87.2
D-proline
-
wild-type
1.51
D-Ser
-
pH 8.3, 37°C, recombinant DAO
2.2
D-Ser
-
mutant enzyme E220D/Y224G
2.83
D-Ser
-
pH 8.3, 25°C
3
D-Ser
-
wild-type enzyme
20.5
D-Ser
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
1.8
D-serine
-
mutant T317A
2.5
D-serine
pH 8.5, 25°C, recombinant EGFP-DAAO
3
D-serine
-
at pH 7.0 and 25°C
3
D-serine
pH 8.5, 25°C, recombinant wild-type DAAO
4
D-serine
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
6.08
D-serine
mutant P219L, pH 8.0, 25°C
6.4
D-serine
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
6.55
D-serine
wild-type, pH 8.0, 25°C
8.6
D-serine
wild-type, pH 8.5, 25°C
9.9
D-serine
mutant R120E, pH 8.5, 25°C
15.6
D-serine
mutant R120L, pH 8.5, 25°C
1.75
D-Thr
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
7.6
D-Thr
at pH 8.0 and 60°C
7.7
D-Trp
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
31
D-Trp
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
33
D-Trp
-
mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
42.4
D-Trp
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
3.2
D-tryptophan
-
at pH 7.0 and 25°C
3.7
D-tryptophan
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
15.9
D-Tyr
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
22.5
D-Tyr
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
53
D-Tyr
at pH 8.0 and 60°C
72
D-Tyr
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
14.8
D-tyrosine
-
at pH 7.0 and 25°C
14.83
D-tyrosine
in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C
0.25
D-Val
-
mutant enzyme G222D/Y224G
0.433
D-Val
-
mutant enzymeY224G
0.75
D-Val
-
mutant enzyme R221D/Y224G
1.05
D-Val
-
mutant enzyme E220D/Y224G
2.5
D-Val
-
wild-type enzyme
11.5
D-Val
-
mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
14.6
D-Val
-
mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
31.4
D-Val
at pH 8.0 and 60°C
85.3
D-Val
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C
0.9
D-valine
-
mutant T317A
8.67
D-valine
-
D isotope
0.6
Gly
-
pH 8.3, 25°C
0.09
L-Ala
-
at pH 7.0 and 37°C
9.4
L-Ala
-
at pH 9.8 and 37°C
0.4
L-Pro
-
at pH 8.5 and 37°C
0.7
L-Pro
-
at pH 7.5 and 37°C
6.71
L-Pro
-
at pH 8.0 and 37°C
40
O2
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
82
O2
-
pH 8.5, 25°C, mutant enzyme S335G
120
O2
pH 8.5, 25°C, mutant enzyme Y238S
125
O2
pH 8.5, 25°C, mutant enzyme Y238F
350
O2
-
pH 8.5, 25°C, wild-type enzyme
350
O2
pH 8.5, 25°C, wild-type enzyme
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0.0088
([4-[(3,4-dichloro-5-methyl-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.00039
([4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0052
([4-[(4,5-dichloro-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0067
([4-[(4-bromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl]amino)acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0057
1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.005
1,4-dihydropyrrolo[3,2-c]pyrazole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.000745
1H-indole-2-carboxylic acid
Homo sapiens
-
0.005
1H-pyrrole-2-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2,3-dimethyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
1
2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylic acid
Sus scrofa
-
at pH 8.2 and 37°C
0.005
2-(2,4-dichlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.04
2-(3,3-dimethylbutyl)-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.005
2-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0051
2-benzyl-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.005
2-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-chloro-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
2-phenyl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0005
2-[(3,4-dichlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0007
2-[(4-chlorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0008
2-[(4-fluorophenoxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.02
2-[(benzyloxy)methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.00044
2-[2-(1H-benzimidazol-1-yl)ethyl]-6-hydroxy-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00036
2-[[(1Z)-1-chloroprop-1-en-1-yl]sulfanyl]prop-2-enoic acid
Homo sapiens
pH 8.5, 23°C
-
0.0001
2-[[(3,4-dichlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
2-[[(4-chlorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0003
2-[[(4-fluorophenyl)sulfanyl]methyl]-5-hydroxy-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.005
3-(3-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.005
3-(4-chlorophenyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0001
3-(benzylsulfanyl)-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.005
3-(hydroxymethyl)-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.00007
3-benzyl-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001426
3-chloro-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.001153
3-cyano-4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.000128
3-hydroxy-1,5-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000032 - 0.003081
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
0.000784
3-hydroxy-1,7-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000008 - 0.000424
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
0.0173
3-hydroxy-4-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0000039
3-hydroxy-5-(2-phenylethyl)pyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.00014
3-hydroxy-5-methylpyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000016 - 0.00847
3-hydroxy-5-methylquinolin-2(1H)-one
0.00275
3-hydroxy-6-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000197
3-hydroxy-7-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000038
3-hydroxy-8-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0015
3-hydroxypyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000004 - 0.000215
3-hydroxyquinolin-2(1H)-one
0.000004
3-hydroxyquinolin-2-(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000043 - 0.0001
3-hydroxyquinolin-2-one
0.000004
3-hydroxyquinoline-2-(1H)-one
Homo sapiens
-
at pH 7.0 and 25°C
0.005
3-pyridin-3-yl-4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.0006
3-[(cyclohexylmethyl)sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
3-[[(1,2-benzoxazol-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00006
3-[[(2H-1,3-benzodioxol-5-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
3-[[(3,4-dichlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
3-[[(4-chlorophenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-[[(4-tert-butylphenyl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
3-[[(6-fluoronaphthalen-2-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
3-[[([1,1'-biphenyl]-3-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00009
3-[[([1,1'-biphenyl]-4-yl)methyl]sulfanyl]-5-hydroxy-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000343
4,5-dichlorofuran-2-carboxylic acid
Homo sapiens
-
0.00009
4,5-dichlorothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0073
4,5-dimethylthiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0013
4-(difluoromethyl)thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.1
4-(trifluoromethyl)-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
IC50 above 0.1 mM
0.00782
4-fluoro-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.0000049
4-hydroxy-6-(1-phenylethyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000038
4-hydroxy-6-(2-phenylethyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000013
4-hydroxy-6-(3-phenylpropyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000022
4-hydroxy-6-(phenoxymethyl)pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000021
4-hydroxy-6-[2-(3-methoxyphenyl)ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000029
4-hydroxy-6-[2-(4-methoxyphenyl)ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000112
4-hydroxy-6-[2-(7-hydroxy-2-oxo-4-phenyl-2H-1-benzopyran-6-yl)ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.0000084
4-hydroxy-6-[2-[2-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000024
4-hydroxy-6-[2-[3-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000012
4-hydroxy-6-[2-[4-(trifluoromethyl)phenyl]ethyl]pyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000073
4-hydroxy-6-[2-[7-hydroxy-4-(3-methoxyphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000052
4-hydroxy-6-[2-[7-hydroxy-4-(3-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000474
4-hydroxy-6-[2-[7-hydroxy-4-(4-methylphenyl)-2-oxo-2H-1-benzopyran-6-yl]ethyl]pyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.0013
4-methylthiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000238
4-[2-(4-chlorophenyl)ethyl]-1H-pyrrole-3-carboxylic acid
Homo sapiens
-
0.0000014 - 0.000141
4H-furo[3,2-b]pyrrole-5-carboxylic acid
0.005
4H-pyrrolo[2,3-d][1,3]oxazole-5-carboxylic acid
Homo sapiens
IC50 above 0.005 mM
0.000516
4H-pyrrolo[2,3-d][1,3]thiazole-5-carboxylic acid
Homo sapiens
-
0.004204
4H-pyrrolo[3,2-d][1,3]thiazole-5-carboxylic acid
Homo sapiens
-
0.000114 - 0.000145
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
0.000145
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
0.000145 - 0.000245
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
0.0088
5-(difluoromethyl)thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.021
5-(trifluoromethyl)thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000599
5-bromo-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.0013
5-bromothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000047
5-chloro-3-hydroxypyridin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000004 - 0.00004
5-chloro-3-hydroxyquinolin-2(1H)-one
0.000003 - 0.000004
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
0.000005 - 0.00005
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
0.00072
5-chlorothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.000008 - 0.003665
5-ethyl-3-hydroxyquinolin-2(1H)-one
0.000008 - 0.000196
5-fluoro-3-hydroxyquinolin-2(1H)-one
0.0014
5-fluorothiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.0005
5-hydroxy-2-(2-phenylethyl)-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.05
5-hydroxy-2-(methoxymethyl)-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0009
5-hydroxy-2-(phenoxymethyl)-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0009
5-hydroxy-2-[(naphthalen-1-yloxy)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0008
5-hydroxy-2-[(naphthalen-2-yloxy)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
5-hydroxy-2-[(phenylsulfanyl)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.003
5-hydroxy-2-[(pyridin-3-yloxy)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.004
5-hydroxy-2-[(pyrimidin-2-ylsulfanyl)methyl]-4H-pyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.00006
5-hydroxy-3-(2-phenylethyl)-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.004
5-hydroxy-3-(3-phenylpropyl)-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.04
5-hydroxy-3-[(2-phenylethyl)sulfanyl]-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
5-hydroxy-3-[[(4-iodophenyl)methyl]sulfanyl]-1,2,4-triazin-6(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00151
5-iodo-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.000901 - 0.00091
5-methylpyrazole-3-carboxylic acid
0.0046
5-methylthiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
-
0.00295
5-nitro-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.0000047
6-(2-cyclohexylethyl)-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.00067
6-(3,3-dimethylbutyl)-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.3
6-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.005
6-(trifluoromethyl)-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.000507
6-chloro-1,2-benzisoxazol-3-ol
Homo sapiens
-
0.0203
6-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.000155
6-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00009 - 0.00021
6-chlorobenzo[d]isoxazol-3-ol
0.0003
6-cyclohexyl-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.1
6-ethoxy-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
IC50 above 0.1 mM
0.1
6-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.000444
6-fluoro-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.000009 - 0.000308
6-fluoro-3-hydroxyquinolin-2(1H)-one
0.0001
6-hydroxy-2-(2-(naphthalen-1-yl)ethyl)-1,2,4-triazine-3,5-(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00007
6-hydroxy-2-(2-phenylethyl)-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00026
6-hydroxy-2-(3-methylbutyl)-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.0017
6-hydroxy-2-(3-phenylpropyl)-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.0028
6-hydroxy-2-methyl-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.1
6-hydroxy-2-phenyl-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00005
6-hydroxy-2-[(naphthalen-1-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00022
6-hydroxy-2-[(naphthalen-2-yl)methyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00033
6-hydroxy-2-[2-(1H-pyrazol-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00031
6-hydroxy-2-[2-(1H-pyrrolo[2,3-b]pyridin-1-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00076
6-hydroxy-2-[2-(pyridin-2-yl)ethyl]-1,2,4-triazine-3,5(2H,4H)-dione
Homo sapiens
-
at pH 8.5 and 25°C
0.00257
6-methoxy-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.1
6-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.000269
6-methyl-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.0177
6-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.000722
6-nitro-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.3
6-phenethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00012
6-[(E)-2-(4-chlorophenyl)vinyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000002
6-[2-(2-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000015
6-[2-(3,5-difluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000013
6-[2-(3,5-dimethoxyphenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000014
6-[2-(3-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000027
6-[2-(4-chlorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.0000031
6-[2-(4-fluorophenyl)ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000063
6-[2-[3,5-bis(trifluoromethyl)phenyl]ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000069
6-[2-[4-(3-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000119
6-[2-[4-(4-chlorophenyl)-7-hydroxy-2-oxo-2H-1-benzopyran-6-yl]ethyl]-4-hydroxypyridazin-3(2H)-one
Homo sapiens
pH 8, 37°C
-
0.000269
6H-thieno[2,3-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.00053
7,8-dibromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00065
7,8-dichloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0124
7-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00048
7-bromo-8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0004
7-bromo-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0067
7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0001
7-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00026 - 0.00416
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
0.0226
7-ethyl-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.023
7-fluoro-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
-
0.00046
7-fluoro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00001 - 0.001445
7-fluoro-3-hydroxyquinolin-2(1H)-one
0.1
7-fluoro-6-(trifluoromethyl)-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
IC50 above 0.1 mM
0.00015 - 0.00034
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
0.05
7-hydroxypyrido[2,3-b]pyrazin-6(5H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.1
7-methyl-1,2-benzisoxazol-3-ol
Rattus norvegicus
-
IC50 above 0.1 mM
0.0367
7-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0229
7-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.3
8-(benzyloxy)-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00022 - 0.00224
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
0.00024 - 0.00799
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
0.00014 - 0.00021
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
0.000033 - 0.00872
8-chloro-3-hydroxyquinolin-2(1H)-one
0.1
8-ethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0024
8-ethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0144
8-ethyl-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000003 - 0.00018
8-fluoro-3-hydroxyquinolin-2(1H)-one
0.1
8-isopropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0857
8-methoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00063
8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
1
8-phenoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.3
8-phenylethoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.3
8-phenylpropoxy-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00052
8-trifluoromethyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.016
benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.00188
benzo[d]isoxazol-3-ol
Rattus norvegicus
-
-
0.002
kojic acid
Homo sapiens
pH and temperature not specified in the publication
1
methyl 2,3-dioxo-1,2,3,4-tetrahydropyrido[2,3-b]pyrazine-7-carboxylate
Sus scrofa
-
at pH 8.2 and 37°C
300
NaCl
Trigonopsis variabilis
-
in 100 mM potassium phosphate buffer pH 8.0, at 30°C
0.0336
quinoxaline-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.0078
thiophene-2-carboxylic acid
Homo sapiens
pH 8.5, 23°C
0.00049
[[4-[(4,5-dibromo-1H-pyrrole-2-carbonyl)amino]-1H-pyrrole-2-carbonyl](methyl)amino]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
additional information
additional information
-
0.000032
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.003081
3-hydroxy-1,6-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000008
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000009
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0002
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000424
3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000016
3-hydroxy-5-methylquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00847
3-hydroxy-5-methylquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000004
3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.0000069
3-hydroxyquinolin-2(1H)-one
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000215
3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000043
3-hydroxyquinolin-2-one
Homo sapiens
-
at pH 8.2 and 37°C
0.000094
3-hydroxyquinolin-2-one
Rattus norvegicus
-
at pH 8.2 and 37°C
0.0001
3-hydroxyquinolin-2-one
Sus scrofa
-
at pH 8.2 and 37°C
0.0000014
4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
in 50 mM potassium phosphate buffer (pH 7.5), at 22°C
0.000141
4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.000141
4H-furo[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
at pH 7.0 and 25°C
0.000114
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
Rattus norvegicus
-
-
0.000145
4H-thieno [3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
-
0.000145
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
Homo sapiens
-
-
0.000145
4H-thieno[3,2-b] pyrrole-5-carboxylic acid
Rattus norvegicus
-
-
0.000145
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
at pH 7.0 and 25°C
0.000245
4H-thieno[3,2-b]pyrrole-5-carboxylic acid
Homo sapiens
-
0.000004
5-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00004
5-chloro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000003
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000004
5-chloro-6-fluoro-3-hydroxy-1,8-naphthyridin-2(1H)-one hydrobromide
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000005
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00005
5-chloro-6-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000008
5-ethyl-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.003665
5-ethyl-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000008
5-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000196
5-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000901
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
-
0.000901
5-methylpyrazole-3-carboxylic acid
Rattus norvegicus
-
-
0.00091
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
0.00091
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
at pH 7.0 and 25°C
0.00091
5-methylpyrazole-3-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00009
6-chlorobenzo[d]isoxazol-3-ol
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00011
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
at pH 8.2 and 37°C
0.00018
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
at pH 7.0 and 25°C
0.000188
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
-
0.000188
6-chlorobenzo[d]isoxazol-3-ol
Rattus norvegicus
-
-
0.00019
6-chlorobenzo[d]isoxazol-3-ol
Homo sapiens
-
pH and temperature not specified in the publication
0.00021
6-chlorobenzo[d]isoxazol-3-ol
Sus scrofa
-
at pH 8.2 and 37°C
0.000009
6-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.000308
6-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00026
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00113
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.00416
7-chloro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00001
7-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.001445
7-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.00015
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00015
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00034
7-fluoro-8-methyl-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.00022
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00023
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.00224
8-bromo-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00024
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00138
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.00799
8-bromo-7-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00014
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Rattus norvegicus
-
at pH 8.2 and 37°C
0.00018
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Sus scrofa
-
at pH 8.2 and 37°C
0.00021
8-chloro-1,4-dihydropyrido[2,3-b]pyrazine-2,3-dione
Homo sapiens
-
at pH 8.2 and 37°C
0.000033
8-chloro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00872
8-chloro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
0.000003
8-fluoro-3-hydroxyquinolin-2(1H)-one
Homo sapiens
pH 8.5, recombinant enzyme, with substrate D-serine
0.00018
8-fluoro-3-hydroxyquinolin-2(1H)-one
Rattus norvegicus
-
pH 8.5, recombinant enzyme, with substrate D-serine
additional information
additional information
Homo sapiens
IC50 with substrate D-aspartate, overview
-
additional information
additional information
Homo sapiens
-
IC50 with substrate D-aspartate, overview
-
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G183R
inactive apoprotein, substitution negatively affects the ability to bind the flavin cofactor in the correct orientation. The overexpressed G183R protein is not fully targeted to peroxisomes, shows colocalization with ubiquitin, and increases 7fold both the D-serine cellular concentration and the D/(D+L)-serine ratio
G72
-
the truncation mutant shows enhanced enzyme activity
G72123-153
-
the truncation mutant shows enhanced enzyme activity
G72138-153
-
the truncation mutant shows enhanced enzyme activity
L56T
increase in activity towards D-alanine, decrease in activity towards D-serine, D-tryptophan
P219L
mutation to corresponding residue of porcine DAO. The turnover numbers (kcat) of P219L are unchanged, but its Km values are decreased compared with wild-type, leading to an increase in the catalytic efficiency (kcat/Km). Benzoate inhibits P219L with lower Ki value
R120E
substitution in order to mimic the active nuclear translocation signal, slightly alters protein conformation, thermal stability, and kinetic properties, while the dimeric structure and the ligand-binding properties are unchanged. Mutant shows an increase in cytosolic localization that promotes nuclear targeting, without affecting cell viability
R120L
substitution in order to eliminate the positive charge, slightly alters protein conformation, thermal stability, and kinetic properties, while the dimeric structure and the ligand-binding properties are unchanged
Y55A
slight reduction in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan, D-histidine, D-methionine, D-phenylalanine, D-tyrosine
Y55A/L56T
about 40-60% reduction in activity towards D-alanine, D-serine, slight reduction in activity towards D-tryptophan
Y55W
20-40% reduction in activity towards D-alanine, D-serine, no change in activity towards D-tryptophan
Y55W/L56T
50-70% reduction in activity towards D-alanine, D-serine, no change in activity towards D-tryptophan
G181R/D481N
compared to animals with only the Grin1D481N mutation, mice with both the Dao1G181R and Grin1D481N mutations display an improvement in social approach and spatial memory retention, as well as a reversal of abnormally persistent latent inhibition and a partial normalization of startle responses
D481N
-
homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
-
G181R
-
homozygous Dao1G181R mutant mice that lack function of the D-serine catabolic enzyme DAO display an elevation in anxiety, homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit also an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
-
D242V/Q253R/D304V
mutant with altered substrate specificity
DELTAS308-K321
deletion of 14 amino acids from Ser308 to Lys321 in a surface loop (connecting beta-strands 12 and 13) transforms the enzyme from a dimeric protein into a stable monomer. The mutant enzyme is still catalytically competent and retains its binding with the FAD coenzyme. The Kd value of the apoprotein-FAD complex is 5fold higher than that of the wild-type enzyme. 1.9fold increase in Km-value for D-Ala, 1.8fold decrease in Vmax value with D-Trp
G52V
site-directed mutagenesis, in the mutant the reactivity of the reduced enzyme with O2 is decreased about 100fold and the turnover number about 1000fold compared to the wild-type enzyme
L118H
mutant with altered substrate specificity
M213R/Y238R
the ratio of turnover number to Km-value for D-Asp is 36.6fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Ala is 1000fold lower than that of the wild-type enzyme
Q339N
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
R285A
-
decreased activity with D-amino acids
R285D
-
decreased activity with D-amino acids
R285K
-
decreased activity with D-amino acids
R285Q
-
decreased activity with D-amino acids
S19G/S120P/Q144R/K321M/A345V
S335H
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
S335R
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
T60A/Q144R/K152E
-
increased overall activity compared to the wild type enzyme
W243I
mutant ezyme with a significantly lower content of flavin cofactor. Loss of the tertiary structure elements and of the flavin cofactor occurs at lower temperatures in mutant than in the dimeric wild-type enzyme. The midpoint concentration of urea required for unfolding is significanlty lower than for the wild-type enzyme
W243Y
mutant enzyme retains the FAD coenzyme. Loss of the tertiary structure elements and of the flavin cofactor occurs at lower temperatures in mutant than in the dimeric wild-type enzyme
Y223F
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
E222D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
F42C
-
mutant retains more than 70% of activity after 1 h, while the wild-type enzyme retains only 10% activity. Optimal temperature of mutant enzyme is about 10°C higher than that of wild-type enzyme. Activity at the optimal temperature is about 20% higher than that of wild-type enzyme. KM-values for D-Ala, D-Met, D-Phe and D-Ser are 40-50% of the wild-type value
H307L
Kd for FAD is 28fold higher with respect to the wild type enzyme while activity is mostly retained
I230A/R283G
mutant accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate, activity with (R)-1-phenylethylamine is diminished 10fold as compared with the Y228L/R283G variant
I230C/R283G
accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate
I230F/R283G
accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate
R221D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
R283G
mutant has completely lost the activity for D-amino acids but accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate
T317A
-
decreased activity to FAD
T56L
decrease in activity towards D-alanine, increase in activity towards D-serine, D-tryptophan
Y224F
-
turnover numbers similar to wild-type
Y228L
about 20% of wild-type activity wih phenylalanine
Y228L/F242I/R283G
mutant is able to oxidize 1-(2-naphthyl)ethylamine
Y55A
strong reduction in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan, D-phenylalanine, D-tyrosine, D-arginine
Y55A/T56L
decrease in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan
Y55W
strong reduction in activity towards D-alanine, D-serine, increase in activity towards D-tryptophan
Y55W/T56L
increase in activity towards D-alanine, D-tryptophan, D-arginine, D-cysteine, D-phenylalanine, D-tyrosine, decrease in activity towards D-serine
C106C108-(SO2H)
-
oxidatively modified enzyme shows 75% loss of activity
C108D
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108D, overview
C108S
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108S, overview
D206A
-
decreased activity with D-amino acids
D206E
-
decreased activity with D-amino acids
D206G
-
no activity with D-amino acids
D206L
-
no activity with D-amino acids
D206N
-
no activity with D-amino acids
D206S
-
decreased activity with D-amino acids
F258A
-
the improvement of catalytic efficiency with D-Tyr, D-Phe, and D-Leu for mutant enzyme F258A is 3.66, 11.7, and 1.5fold, respectively. The mutant is inactive with D-Ala, D-Ser, D-Lys, and D-Thr, while the activity with D-Tyr, D-Leu and especially with D-Phe significantly increases
F258S
-
the improvement of catalytic efficiency with D-Tyr, D-Phe, and D-Leu for mutant enzyme F258S is 1.7, 4.75, and 6.61fold, respectively. The mutant is inactive with D-Ala, D-Ser, D-Lys, and D-Thr, while the activity with D-Tyr, D-Leu and especially with D-Phe significantly increases
F258Y
-
the mutant is inactive with D-Val, D-Tyr, D-Ala, D-Ser, D-Lys, and D-Thr
F54A
site-directed mutagenesis
F54S
site-directed mutagenesis
F54Y
site-directed mutagenesis, the mutant shows 6fold improvement in kcat,app and about 2.5fold increase in Ki of glutaryl-7-aminocephalosporanic acid, the substitution improves the catalytic activity and thermostability of mutant DAAO compared to the wild-type enzyme. Heat treatment at 55° for 60 min does not decrease the activity of F54Y. The Tyr substitution might initiate hydrogen bond formation with the amino group of CPC and facilitate deamination
M156L
mutant shows increased H2O2 resistance
M209L
mutant shows increased H2O2 resistance
R110A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme, but shows increased temperature denaturation. Release of FAD is the dominant path of thermal denaturation of R110A
Y223F
-
slower substrate binding than the wild-type
C108D
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108D, overview
-
C108S
-
site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant releases the cofactor in a quasi-irreversible manner and is therefore not stabilized by external FAD against loss of activity. Conformational properties and kinetics of C108S, overview
-
R110A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme, but shows increased temperature denaturation. Release of FAD is the dominant path of thermal denaturation of R110A
-
G281C
inactive
G281C
-
decreased activity with D-amino acids
R199W
-
naturally occuring mutation, the mutation in the D-amino acid oxidase gene is associated with classical adult onset familial amyotrophic lateral sclerosis the 14.52 cM region on chromosome 12q22-23 is linked to disease. Neuronal cell lines expressing R199W DAO show decreased viability and increased ubiquitinated aggregates compared with cells expressing the wild-type protein, overview. Lentiviral-mediated expression of mutant R199W DAO in primary motor neuron cultures causes increased TUNEL labeling
R199W
transgenic mice overexpressing mutant R199W show marked abnormal motor features, e.g. kyphosis, associated with a significant loss (19%) of lumbar spinal cord motor neurons, analyzed at 14 months. This effect is greater in females. In transgenic mice expressing mutant R199W and superoxide dismutase SOD1 G93A mutant, overall survival is not affected, but the onset of neurological signs is significantly earlier in female double transgenic animals than their female SOD1 G93A littermates
D481N
Grin1D481N mice show deficits in sociability, prolonged latent inhibition, enhanced startle reactivity and impaired spatial memory
D481N
-
homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
G181R
inactive
G181R
-
homozygous Dao1G181R mutant mice that lack function of the D-serine catabolic enzyme DAO display an elevation in anxiety, homozygous Grin1D481N mutant mice with reduced NMDA-NR1 glycine affinity exhibit also an altered anxiety-like behavior. Deficient DAO activity also reverses the anxiolytic effects of diminished NMDAR function in mice carrying both the homozygous Grin1D481N and Dao1G181R mutation, phenotypes, overview
G181R
the hypofunctional Dao1G181R mutation elevates brain levels of D-serine, but alone it does not affect performance in the behavioral measures
G181R
-
naturally occuring missense mutation, inactive mutant
M213E
-
increased overall activity compared to the wild type enzyme
M213E
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
M213G
-
increased overall activity compared to the wild type enzyme
M213G
mutant shows lower activity and substrate specificity constant on the natural aromatic D-amino acids and higher acitivy on artificial amino acids compared to the wild type enzyme
M213R
the ratio of turnover number to Km-value for D-Asp is 74fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Glu is 29.5fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Ala is 172fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Pro is 166fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Asn is 9.4fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Gln is 3.2fold higher than that of the wild-type enzyme, the ratio of turnover number to Km-value for D-Met is 56fold lower than that of the wild-type enzyme
M213R
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increased overall activity compared to the wild type enzyme
M213R
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Q144R
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increased overall activity compared to the wild type enzyme
Q144R
mutant with altered substrate specificity
Q144R
site-directed mutagenesis, the mutant shows reduced activity comapared to the wild-type enzyme
Q339E
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decreased overall activity compared to the wild type enzyme
Q339E
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
S19G/S120P/Q144R/K321M/A345V
library screening and identification of a naturally occuring DAAO mutant with increased activity at low O2 and D-Ala concentrations and a 10fold lower Km for O2
S19G/S120P/Q144R/K321M/A345V
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the mutant possesses a 10fold lower KM,O2, thus resulting in dramatically increased activity at low O2 concentrations
S335G
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mutant enzyme has a lower turnover number with D-Ala than wild-type enzyme. The spectral and ligand binding properties of the mutant are similar to those of the wild-type enzyme
S335G
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y223S
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y223S
strongly decreased turnover number
Y238F
3fold slower turnover on D-Ala as substrate than wild-type enzyme. KM-value for D-Ala is 2fold lower than the wild-type value, Km-value for D-Ser is 4.7fold lower than the wild-type value, Km-value for D-Pro is 1.7fold lower than the wild-type value, Km-value for D-Trp is 1.5fold lower than the wild-type value, Km-value for cephalosporin is 2.6fold lower than the wild-type value, Km-value for D-Val is 3fold lower than the wild-type value, Km-value for D-Phe is 4.3fold lower than the wild-type value
Y238F
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y238F
the mutation decreases the rate of product release und to a lesser extend the rate of substrate binding and does not alter significantly the substrate specificity of the enzyme
Y238R
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increased overall activity compared to the wild type enzyme
Y238R
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y238S
3fold slower turnover on D-Ala as substrate than wild-type enzyme. KM-value for D-Ala is 2fold lower than the wild-type value, Km-value for D-Ser is 8fold lower than the wild-type value, Km-value for D-Pro is 1.6fold lower than the wild-type value, Km-value for D-Trp is identical to wild-type value, Km-value for cephalosporin is 2.6fold lower than the wild-type value, Km-value for D-Val is 3.2fold lower than the wild-type value, Km-value for D-Phe is 7.5fold lower than the wild-type value
Y238S
mutant shows lower activity on neutral and basic amino acids compared to the wild type enzyme
Y238S
the mutation decreases the rate of product release und to a lesser extend the rate of substrate binding and does not alter significantly the substrate specificity of the enzyme
E220D/Y224G
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kcat/KM for D-Arg is 5fold higher than wild-type value, kcat/Km for L-Lys is 2.91fold higher than wild-type value, kcat/KM for D-Ala is 124fold lower than wild-type value, kcat/Km for D-Ser is more than 110fold lower than wild-type value, kcat/Km for D-Pro is 17.5fold lower than wild-type value, kcat/Km for D-Val is 12fold lower than wild-type value, kcat/KM for D-Met is 1.5fold higher than wild-type value, kcat/KM for D-Phe is 3.3fold higher than wild-type value
E220D/Y224G
decreased catalytic activity for D-Ala compared to the wild type enzyme
G313A
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decreased activities to various D-amino acids
G313A
decreased catalytic activity for D-Ala compared to the wild type enzyme
Y228F
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turnover numbers lower than turnover numbers of wild-type
Y228F
50% activity compared to the wild type enzyme, 120fold decreased reduction rate
Y228L/R283G
(R)-alpha-methylbenzylamine as neutral amine is substrate of mutant Y228L/R283G, while an active-site residue, likely Tyr224, must be uncharged for productive binding. The oxidative half-reaction is unperturbed by the mutation and with flavin oxidation preceding product release
Y228L/R283G
mutant accepts 1-(4-chlorophenyl)-1-phenylmethanamine as substrate
Y228L/R283G
mutant displays altered substrate specificity toward (R)-amines acting on alpha-methylbenzylamine and its derivatives, alpha-ethylbenzylamine, alkylamine, and cyclic secondary amines, and totally losing the activities toward the original substrates, D-amino acids
additional information
DAO variants including V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E significantly reduce fluctuations around the active site loop residues and close to the hydrophobic stretch region of residues 47-51. In molecular dynamics simulations, V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E variants exhibit nearly similar radius of gyration, the H78Y, R279Q and S340F variants including the wild-type exhibit a slightly increased profile. Variants V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E experience more compact structure than wild-type and H78Y, R279Q and S340F during the course of simulations
additional information
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DAO variants including V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E significantly reduce fluctuations around the active site loop residues and close to the hydrophobic stretch region of residues 47-51. In molecular dynamics simulations, V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E variants exhibit nearly similar radius of gyration, the H78Y, R279Q and S340F variants including the wild-type exhibit a slightly increased profile. Variants V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E experience more compact structure than wild-type and H78Y, R279Q and S340F during the course of simulations
additional information
mutations in residues located on the loops on the border between the active site and the secondary binding pocket. Mutations modulate substrate specificity, product egress and enzyme activity
additional information
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mutations in residues located on the loops on the border between the active site and the secondary binding pocket. Mutations modulate substrate specificity, product egress and enzyme activity
additional information
comparison of D-Ser and D-Ala contents in different tissues in wild-type DAO+/+ mice with knockout mice DAO-/- and heterozygous DAO+/- mice, detailed overview
additional information
long-term increases in the brain levels of the endogenous N-methyl-D-aspartate receptor, NMDAR, glycine site agonist D-serine, through the genetic inactivation of its catabolic enzyme D-amino acid oxidase in mice
additional information
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construction of a mutant rat strain LEA/SENDAI lacking D-amino-acid oxidase
additional information
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development of an implantable D-serine biosensor for in vivo monitoring using mammalian D-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode, method evaluation, overview
additional information
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DELTAloop mutant in which 14 residues belonging to a loop connecting strands betaF5-beta-F6 have been deleted is monomeric and thermodynamically less stable than dimeric wild-type DAAO, with melting temperatures of 48°C and 54°C, respectively
additional information
for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is physically adsorbed on an electrode surface. For in vivo experiments, the enzyme layer is protected with an additional Nafion membrane
additional information
immobilization of the enzyme onto magnetic nanoparticles stabilizes the enzyme
additional information
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immobilization of the enzyme onto magnetic nanoparticles stabilizes the enzyme
additional information
establishing the transformed Pichia pastoris, expressing RgDAO, as whole-cell catalyst
additional information
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establishing the transformed Pichia pastoris, expressing RgDAO, as whole-cell catalyst
additional information
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for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is adsorbed on a cylindrical platinum microelectrode covered by a layer of poly-m-phenylenediamine, a selective mediator for H2O2
additional information
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immobilization of the enzyme, interaction of D-amino acid oxidase with single-walled carbon nanotubes, analysis by spectroscopic ellipsometry. DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity, highest enzymatic activity by adsorbing the protein at pH 5.7 and 0.1 mg/ml, adsorption kinetics at different pH values, overview
additional information
mutations in residues located on the loops on the border between the active site and the secondary binding pocket. Mutations modulate substrate specificity, product egress and enzyme activity
additional information
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mutations in residues located on the loops on the border between the active site and the secondary binding pocket. Mutations modulate substrate specificity, product egress and enzyme activity
additional information
oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation
additional information
oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation
additional information
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oxidation of Cys108 into cysteine sulfinic acid causes a global conformational response that affects the protein environment of the FAD cofactor. In comparison with the native enzyme, the mutation results in a fourfold-decreased specific activity, reflecting a catalytic efficiency for reduction of dioxygen lowered by about the same factor, and a markedly decreased propensity to aggregate under conditions of thermal denaturation
additional information
construction of point mutants with altered substrate specificity compared to the wild-type enzyme, the created mutant forms of TvDAAO are perfectly suitable for selective determination of D-Ser in excess of D-Ala, D-Asp, and D-Pro
additional information
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immobilization of the recombinant enzyme on solid beads through affinity of its N-terminal Strep-tag to Strep-Tactin coated on insoluble particles, covalent attachment, re-usable in multiple cycles of substrate conversion, the surfactant Pluronic F-68 stabilizes DAO by protecting the enzyme from the deleterious effect of gas-liquid interfaces
additional information
development of a robust and highly active Pichia pastoris TvDAO whole-cell biocatalyst in a multistep engineering process for use in cephalosporin C conversion on industrial scale, overview. Usage of a fed-batch cultivation of the multicopy strain
additional information
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development of a robust and highly active Pichia pastoris TvDAO whole-cell biocatalyst in a multistep engineering process for use in cephalosporin C conversion on industrial scale, overview. Usage of a fed-batch cultivation of the multicopy strain
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