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(R)-2-hydroxybutanoate + 2,6-dichlorophenolindophenol
2-oxobutanoate + reduced 2,6-dichlorophenolindophenol
preferred substrate
-
-
?
(R)-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
preferred substrate
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
(S)-lactate + O2
pyruvate + H2O2
2-hydroxy-3-methylvalerate + O2
?
-
A95G-mutant
-
-
?
2-hydroxybutanoate + bromopyruvate + ?
bromolactate + pyruvate + ?
-
transhydrogenation reaction
-
?
2-hydroxybutyrate + O2
?
-
wild-type and A95G-mutant
-
-
?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
-
-
-
?
2-hydroxydodecanoate + O2
2-oxododecanoate + H2O2
-
-
-
?
2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
2-hydroxyisovalerate + O2
?
-
A95G-mutant
-
-
?
2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxo-octanoate + reduced 2,6-dichlorophenolindophenol
-
-
-
r
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
2-hydroxyvalerate + O2
?
-
wild-type and A95G-mutant
-
-
?
2-mercaptoethanol-glyoxylate adduct + O2
?
-
-
-
-
r
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
coenzyme A-glyoxylate adduct + O2
?
-
-
-
-
r
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
D-lactate + O2
pyruvate + H2O2
DL-2-hydroxy-3-butynoate + O2
2-oxo-3-butynoate + H2O2
-
good substrate, but inactivation after 25 turnovers
-
?
DL-2-hydroxy-3-heptynoate + O2
2-oxo-3-heptynoate + H2O2
-
86% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-hexynoate + O2
2-oxo-3-hexynoate + H2O2
-
65% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
-
70% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-pentynoate + O2
2-oxo-3-pentynoate + H2O2
-
2fold higher activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-4-methylmercaptobutyrate + 2,6-dichlorophenolindophenol
2-oxo-4-methylmercaptobutyrate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, low activity for short chain oxidase
-
?
DL-2-hydroxy-4-methylthiobutanoic acid + 2,6-dichlorophenolindophenol
2-oxo-4-methylthiobutanoic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-2-hydroxybutyrate + 2,4-dinitrophenylhydrazine
2-oxobutyrate 2,4-dinitrophenylhydrazone + ?
-
low activity
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol
2-oxocaproate + reduced 2,6-dichlorophenolindophenol
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
DL-2-hydroxydecanoate + 2,6-dichlorophenolindophenol
2-oxodecanoate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, traces of activity for short chain oxidase
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
DL-2-hydroxyisovalerate + 2,4-dinitrophenylhydrazine
2-oxoisovalerate 2,4-dinitrophenylhydrazone + ?
-
very low activity
-
?
DL-2-hydroxyisovalerate + 2,6-dichlorophenolindophenol
2-oxoisovalerate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
DL-2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxooctanoate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol
2-oxovalerate + reduced 2,6-dichlorophenolindophenol
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
DL-3-indolelactate + 2,6-dichlorophenolindophenol
3-indolepyruvate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-3-indolelactate + O2
3-indolepyruvate + H2O2
-
-
-
?
DL-3-methoxy-4-hydroxymandelate + 2,6-dichlorophenolindophenol
(3-methoxy-4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-alpha-phenyllactate + O2
? + H2O2
-
-
-
-
r
DL-beta-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
DL-glycerate + O2
?
-
-
-
-
r
DL-glycerate + O2
? + H2O2
-
-
-
?
DL-lactate + O2
pyruvate + H2O2
-
-
-
?
DL-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
low activity
-
?
DL-mandelate + O2
phenylglyoxylic acid + H2O2
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-methionine + O2
? + H2O2
-
-
-
?
DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol
(4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
DL-p-hydroxymandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
-
90% of the activity compared to DL-2-hydroxybutyrate
-
?
glycolate + 2,4-dinitrophenylhydrazine
glyoxylate 2,4-dinitrophenylhydrazone + ?
-
best substrate tested
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
glycolate + acceptor
glyoxylate + reduced acceptor
glycolate + ferricyanide
glyoxylate + ferrocyanide
glycolate + O2
glyoxylate + H2O2
glycolate + phenazine methosulfate
glyoxylate + reduced phenazine methosulfate
-
-
-
?
glycolate + phenylhydrazine
glyoxylate + phenylhydrazone
-
-
-
?
glyoxalate + O2
oxalate + H2O2
-
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
glyoxylate + ferricyanide
? + ferrocyanide
-
-
-
?
glyoxylate thiohemiacetals + O2
? + H2O2
-
possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
-
?
homoserine + O2
? + H2O2
-
traces of activity
-
?
isoleucic acid + O2
? + H2O2
-
-
-
?
L-2-hydroxy octanoate + O2
2-oxo-octanoate + H2O2
-
-
-
?
L-2-hydroxy palmitate + O2
2-oxo-palmitate + H2O2
-
-
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
-
oxidative decarboxylation
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
L-2-hydroxyisocaproate + 2,4-dinitrophenylhydrazine
2-oxoisocaproate 2,4-dinitrophenylhydrazone + ?
-
-
-
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
L-2-hydroxyisocaproate + O2
4-methyl-2-oxopentanoate + H2O2
-
100% activity with long chain oxidase, 32% activity with short chain oxidase
-
-
r
L-2-hydroxyphenyllactate + O2
? + H2O2
L-4-chloromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-fluoromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methoxymandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methylmandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-nitromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-trifluoromethylmandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-alanine + O2
? + H2O2
-
low activity
-
?
L-alpha-hydroxy-isovalerate + O2
3-methyl-2-oxobutanoate + H2O2
-
-
-
-
r
L-alpha-hydroxyphenyllactate + O2
? + H2O2
-
-
-
-
r
L-isoleucine + O2
? + H2O2
-
low activity
-
?
L-lactate + 2,4-dinitrophenylhydrazine
pyruvate 2,4-dinitrophenylhydrazone + ?
-
very low activity
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
L-lactate + O2
pyruvate + H2O2
L-lactate + phenazine methosulfate
? + reduced phenazine methosulfate
-
-
-
?
L-lactate + phenylhydrazine
pyruvate + phenylhydrazone
-
-
-
?
L-leucine + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-lysine + O2
? + H2O2
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
L-mandelate + O2
? + H2O2
-
-
-
?
L-methionine + O2
? + H2O2
L-phenylalanine + O2
? + H2O2
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
L-tryptophan + O2
? + H2O2
L-tyrosine + O2
? + H2O2
-
-
-
?
L-valine + O2
? + H2O2
-
low activity
-
?
lactate + O2
pyruvate + H2O2
mandelate + O2
phenylpyruvate + H2O2
oxidation of an L-2-hydroxy acid to a 2-oxoacid, model for the binding of L-mandelate into the active site, overview
-
-
?
N-acetylcysteamine-glyoxylate adduct + O2
?
-
-
-
-
r
pantetheine-glyoxylate adduct + O2
?
-
-
-
-
r
propane-1,3-dithiol-glyoxylate adduct + O2
?
-
-
-
-
r
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
may be the physiological substrates
-
?
valic acid + O2
? + H2O2
-
-
-
?
additional information
?
-
(S)-lactate + O2
acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
glucose-repressible lactate oxidase is likely responsible for H2O2 production
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
48% of the activity compared to glycolate
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
low activity for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
68% of the activity compared to glycolate
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
higher affinity with C5 and C6 hydroxy acids
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
low activity
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
39% of the activity compared to glycolate
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
low activity
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
-
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
-
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
best substrate tested
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
-
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
-
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
-
-
-
?
glycerate + O2
? + H2O2
-
-
-
?
glycerate + O2
? + H2O2
-
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
highest activity for short chain oxidase, no activity for long chain oxidase
-
?
glycolate + acceptor
glyoxylate + reduced acceptor
-
-
-
?
glycolate + acceptor
glyoxylate + reduced acceptor
-
-
-
-
?
glycolate + ferricyanide
glyoxylate + ferrocyanide
-
-
-
?
glycolate + ferricyanide
glyoxylate + ferrocyanide
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
the catalytic adduct is formed by hydrogen abstraction from the re-face of glycolate
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
best substrate
-
-
?
glycolate + O2
glyoxylate + H2O2
plant
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
-
isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
-
?
glycolate + O2
glyoxylate + H2O2
-
preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glyoxylate + O2
? + H2O2
-
substrate for isoenzyme HAOX1
-
?
glyoxylate + O2
? + H2O2
-
26% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
glyoxylate + O2
? + H2O2
-
in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
40% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyphenyllactate + O2
? + H2O2
-
-
-
?
L-2-hydroxyphenyllactate + O2
? + H2O2
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
lower activity for preparation from "heavy" mitochondria
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
-
high activity, does not act on D-lactate
-
?
L-leucine + O2
? + H2O2
-
-
-
?
L-leucine + O2
? + H2O2
-
-
-
?
L-leucine + O2
? + H2O2
-
highest activity
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-mandelate + O2
?
-
A95G-mutant is also reactive
-
-
?
L-mandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-methionine + O2
? + H2O2
-
-
-
?
L-methionine + O2
? + H2O2
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
?
additional information
?
-
no substrates: D-alanine, pyruvate, D-glucose, L-alanine, ethanol and L-lactate
-
-
-
additional information
?
-
-
no substrate: oxalate, acetate, pyruvate, glycerol, propionate, succinate, fumarate, malate, maleate, tartrate, oxaloacetate, 2-oxoglutarate, glycocol,L-alanine, serine, glutamate, ascorbate, glucose, and fructose
-
-
?
additional information
?
-
-
no substrate: glyoxylate. Enzyme also catalyzes the oxidation of short-chain alcohols, reaction of EC 1.1.3.13
-
-
-
additional information
?
-
-
interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
-
-
?
additional information
?
-
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
?
additional information
?
-
-
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
?
additional information
?
-
the enzyme is involved in the photorespiration process
-
-
?
additional information
?
-
the enzyme is not able to metabolize D-lactate
-
-
?
additional information
?
-
-
the enzyme is not able to metabolize D-lactate
-
-
?
additional information
?
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
?
additional information
?
-
-
the enzyme is involved in the photorespiration process
-
-
?
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
?
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
?
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2,6-dichlorophenolindophenol
-
inhibition by excess substrate
2-hydroxybutynoate
-
inhibition of transhydrogenation reaction
2-oxobutyrate
-
non-competitive inhibition at 5 mM
2-oxoisocaproate
-
non-competitive inhibition at 5 mM, most active inhibitor of 2-keto acids, oxidation of 2-hydroxybutyrate most sensitive
2-oxoisovalerate
-
non-competitive inhibition at 5 mM
2-oxovalerate
-
non-competitive inhibition at 5 mM
2-pyridylhydroxymethanesulfonate
-
strong inhibition between 0.1-1 mM
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-decyl-2,5-dioxo-4-hydroxy-3-pyrroline
-
bound to the active site in the three-dimensional structure
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole
-
bound to the active site in the three-dimensional structure
4-carboxy-5-dodecylsulfanyl-1,2,3-triazole
-
4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole
CCPST
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
arsenate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
Atebrin
-
long chain oxidase, 72-76% inhibition at 1 mM, short chain oxidase: 68-76% inhibition at 1 mM
benzaldehyde
-
50% inhibition at 2 mM
bipyridine
-
strong inhibition
caproate
-
mixed-type non-competitive inhibition
chloride
inhibits the enzyme at high concentrations
Cibacron blue 3GA
-
at a concentration higher than 0.001 mM is a normal competitive inhibitor, at concentrations below 0.001 mM the inhibition is time-, dye- and pH-dependent
cysteine
-
28-38% inhibition of glycolate oxidation at 1 mM
dihydrolipoate
-
competitive inhibition of 2-hydroxybutyrate oxidation
Dithionite
-
reduction of FMN
DL-2-hydroxy-3-butynoate
-
irreversible inactivation after 25 turnovers, covalent addition to the coenzyme
DL-2-hydroxy-3-heptynoate
-
inactivation after18000 turnovers
DL-2-hydroxy-3-hexynoate
-
inactivation after 8500 turnovers
DL-2-hydroxy-3-octynoate
-
inactivation after 15000 turnovers
DL-2-hydroxy-3-pentynoate
-
inactivation after 4800 turnovers
DL-2-hydroxyisocaproate
-
marked inhibition above 50 mM
DL-2-hydroxyvalerate
-
marked inhibition above 50 mM
DL-beta-Phenyllactate
-
short chain oxidase: 10% inhibition of glycolate oxidation, 81% inhibition of L-2-hydroxisocaproate oxidation at 10 mM
DL-Lipoate
-
long chain oxidase, 35% inhibition at 0.24 mM, short chain oxidase: 46-52% inhibition at 0.01 mM
DL-vinylglycolate
-
slight inactivation after 10000 turnovers
hydoxylamine
-
66-67% inhibition at 5 mM
hydroxylamine
-
50% inhibition at 5 mM, competitive
iodoacetamide
-
inhibition at 50 mM
L-phenylalanine
-
long chain oxidase, 43% inhibition at 33 mM
oxamate
-
mixed-type non-competitive inhibition
Quinacrine
-
6% inhibition at 1 mM
rotenone
-
50% inhibition at 0.1 mM
sodium sulfite
-
reduces FMN
trans-cinnamate
-
competitive inhibition
2-Hydroxybutyrate
-
at pH 7.0
2-Hydroxybutyrate
-
long chain oxidase, 13-17% inhibition at 17 mM
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
35% inhibition at 0.010 mM
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-chloromercuribenzoate
-
strong inhibition at 0.01 mM
4-chloromercuribenzoate
-
inhibition at 50 mM
4-chloromercuribenzoate
-
long chain oxidase, 29-42% inhibition at 0.001 mM, short chain oxidase: 70-75% inhibition at 0.001 mM
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
8-hydroxyquinoline
-
50% inhibition at 0.05 mM
8-hydroxyquinoline
-
5-17% inhibition at 1 mM
8-hydroxyquinoline
-
8-17% inhibition at 1 mM
acetate
-
mixed-type non-competitive inhibition
Cu2+
-
nearly complete inhibition at 0.025 mM
Cu2+
-
complete inhibition at 0.025 mM
Cu2+
-
50% inhibition at 0.2 mM
Cu2+
-
short chain oxidase: 86% inhibition at 0.1 mM
diethyldithiocarbamate
-
competitive inhibition
diethyldithiocarbamate
-
51-55% inhibition at 1 mM
diphenylglycolic acid
-
11-17% inhibition at 52 mM
diphenylglycolic acid
-
50% inhibition at 52 mM, competitive
glycolate
-
-
glycolate
-
inhibition by excess substrate
glycolate
-
inhibition above 1.7 mM
glyoxylate
-
inhibition by excess substrate
glyoxylate
substrate inhibition at concentrations above 4 mM
iodoacetate
-
inhibition at 50 mM
iodoacetate
-
long chain oxidase, 31-36% inhibition at 0.1 mM, short chain oxidase: no inhibition
KCN
-
mixed-type inhibitor
KCN
-
30% inhibition of L-2-hydroxyisocaproate oxidation at 1 mM, 91% inhibition of glycolate oxidation at 1 mM
L-leucine
-
competitive inhibition
L-leucine
-
9-12% inhibition at 33 mM
L-Mandelate
-
at pH 7.0
L-Mandelate
-
inhibition by excess substrate
o-Iodosobenzoate
-
46-62% inhibition at 0.1 mM
o-Iodosobenzoate
-
46% inhibition at 0.1 mM
o-Iodosobenzoate
-
long chain oxidase, 95-100% inhibition at 0.1 mM, short chain oxidase: no inhibition
o-phenanthroline
-
strong inhibition between 0.1-1.0 mM
o-phenanthroline
-
5-23% inhibition at 1 mM
o-phenanthroline
-
5-14% inhibition at 1 mM
oxalate
-
at pH 7.0
oxalate
-
mixed-type non-competitive inhibition, increasing inhibitory effects as the number of carbons in aliphatic chains decreases
oxalate
-
competitive inhibition
oxalate
-
18% inhibition of glycolate oxidation, 71% inhibition of glyoxylate oxidation at 0.03 mM
oxalate
-
34% inhibition at 5 mM, competitive
phosphate
-
competitive
phosphate
-
50% inhibition at 0.1 M
phosphate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
propionate
-
mixed-type non-competitive inhibition
pyruvate
-
competitive inhibition
pyruvate
-
26% inhibition at 5 mM
succinate
-
-
succinate
-
mesophyll isoform
additional information
-
development of selective inhibitors of Hao2 from screening of a compound library, overview
-
additional information
-
treatment with 4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid or 4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid results in a significant reduction or attenuation of blood pressure in an established or developing model of hypertension, deoxycorticosterone acetate-treated rats
-
additional information
-
development of selective inhibitors of Hao2 from screening of a compound library, overview
-
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(s)-2-hydroxy-acid oxidase deficiency
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Adenocarcinoma
Cellular mechanism of resistance of human colorectal adenocarcinoma cells against apoptosis-induction by Russell's Viper venom l-amino acid oxidase (Rusvinoxidase).
Adenocarcinoma
In vitro cytotoxicity of L-amino acid oxidase from the venom of Crotalus mitchellii pyrrhus.
Adenocarcinoma
The toxin BjussuLAAO-II induces oxidative stress and DNA damage, upregulates the inflammatory cytokine genes TNF and IL6, and downregulates the apoptotic-related genes BAX, BCL2 and RELA in human Caco-2 cells.
Breast Neoplasms
Apoptosis induction in human breast cancer (MCF-7) cells by a novel venom L-amino acid oxidase (Rusvinoxidase) is independent of its enzymatic activity and is accompanied by caspase-7 activation and reactive oxygen species production.
Carcinoma
Electrochemical immunosensor based on chitosan-gold nanoparticle/carbon nanotube as a ?platform and lactate oxidase as a ?label for detection of CA125 oncomarker?.
Colonic Neoplasms
Cytotoxic, Anti-Proliferative and Apoptosis Activity of l-Amino Acid Oxidase from Malaysian Cryptelytrops purpureomaculatus (CP-LAAO) Venom on Human Colon Cancer Cells.
Colonic Neoplasms
Cytotoxic, Antiproliferative and Apoptosis-inducing Activity of L-Amino Acid Oxidase from Malaysian Calloselasma rhodostoma on Human Colon Cancer Cells.
Colonic Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Colorectal Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Colorectal Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Congenital Hyperinsulinism
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Dehydration
Nitrogen Metabolism in Adaptation of Photosynthesis to Water Stress in Rice Grown under Different Nitrogen Levels.
Edema, Cardiac
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Endometrial Neoplasms
Fraxetin inhibits the proliferation of RL95-2 cells through regulation of metabolism.
Fibrosarcoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Glioma
L-amino acid oxidase (LOX) modulation of melphalan activity against intracranial glioma.
Hyperoxaluria
Effect of Tribulus terrestris on oxalate metabolism in rats.
Hyperoxaluria
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Hyperoxaluria
Potential mechanisms of marked hyperoxaluria not due to primary hyperoxaluria I or II.
Hyperoxaluria, Primary
An Investigational RNAi Therapeutic Targeting Glycolate Oxidase Reduces Oxalate Production in Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type I.
Hyperoxaluria, Primary
CRISPR/Cas9-mediated metabolic pathway reprogramming in a novel humanized rat model ameliorates primary hyperoxaluria type 1.
Hyperoxaluria, Primary
Dual Glycolate Oxidase/Lactate Dehydrogenase A Inhibitors for Primary Hyperoxaluria.
Hyperoxaluria, Primary
Glycolate Oxidase Is a Safe and Efficient Target for Substrate Reduction Therapy in a Mouse Model of Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Hyperoxaluria, Primary
High throughput cell-based assay for identification of glycolate oxidase inhibitors as a potential treatment for Primary Hyperoxaluria Type 1.
Hyperoxaluria, Primary
Inhibition of Glycolate Oxidase With Dicer-substrate siRNA Reduces Calcium Oxalate Deposition in a Mouse Model of Primary Hyperoxaluria Type 1.
Hyperoxaluria, Primary
Lumasiran: First Approval.
Hyperoxaluria, Primary
Metabolism of (13)C5-hydroxyproline in mouse models of Primary Hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase.
Hyperoxaluria, Primary
Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Beta-lyase Plays in Hyperoxaluria.
Hyperoxaluria, Primary
Re: An Investigational RNAi Therapeutic Targeting Glycolate Oxidase Reduces Oxalate Production in Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
Re: CRISPR/Cas9-Mediated Glycolate Oxidase Disruption is an Efficacious and Safe Treatment for Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
Re: Glycolate Oxidase is a Safe and Efficient Target for Substrate Reduction Therapy in a Mouse Model of Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
Therapeutic RNA interference: A novel approach to the treatment of primary hyperoxaluria.
Infections
Expression profile of the fish immune enzyme l-amino acid oxidase (LAAO) after Streptococcus agalactiae infection in zebrafish (Danio rerio).
Infections
l-amino acid oxidase expression profile and biochemical responses of rabbitfish (Siganus oramin) after exposure to a high dose of Cryptocaryon irritans.
Kidney Calculi
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
Kidney Calculi
Purification and characterization of recombinant human liver glycolate oxidase.
Kidney Failure, Chronic
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Leukemia
Cytotoxic proteins of Amanita virosa Secr. mushroom: purification, characteristics and action towards mammalian cells.
Melanoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Myotoxicity
Combined venomics, antivenomics and venom gland transcriptome analysis of the monocoled cobra (Naja kaouthia) from China.
Neoplasms
Antiproliferative Activity of King Cobra (Ophiophagus hannah) Venom l-Amino Acid Oxidase.
Neoplasms
CR-LAAO, an L-amino acid oxidase from Calloselasma rhodostoma venom, as a potential tool for developing novel immunotherapeutic strategies against cancer.
Neoplasms
Dual-Modal Therapeutic Role of the Lactate Oxidase-Embedded Hierarchical Porous Zeolitic Imidazolate Framework as a Nanocatalyst for Effective Tumor Suppression.
Neoplasms
Intra/Extracellular Lactic Acid Exhaustion for Synergistic Metabolic Therapy and Immunotherapy of Tumors.
Neoplasms
Isolation, characterization and screening of the in vitro cytotoxic activity of a novel L-amino acid oxidase (LAAOcdt) from Crotalus durissus terrificus venom on human cancer cell lines.
Neoplasms
King cobra (Ophiophagus hannah) venom L-amino acid oxidase induces apoptosis in PC-3 cells and suppresses PC-3 solid tumor growth in a tumor xenograft mouse model.
Neoplasms
l-Amino acid oxidase from Cerastes vipera snake venom: Isolation, characterization and biological effects on bacteria and tumor cell lines.
Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Neoplasms
l-Amino acid oxidase isolated from Calloselasma rhodostoma snake venom induces cytotoxicity and apoptosis in JAK2V617F-positive cell lines.
Neoplasms
Openwork@Dendritic Mesoporous Silica Nanoparticles for Lactate Depletion and Tumor Microenvironment Regulation.
Neoplasms
Oxidoreductase activities in normal rat liver, tumor-bearing rat liver, and hepatoma HC-252.
Neoplasms
Peroxisome inspired hybrid enzyme nanogels for chemodynamic and photodynamic therapy.
Neoplasms
Repolarization of M2 to M1 macrophages triggered by lactate oxidase released from methylcellulose hydrogel.
Neoplasms
Targeting Tumor Microenvironment by Bioreduction-Activated Nanoparticles for Light-Triggered Virotherapy.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
L-amino acid oxidase isolated from Micrurus mipartitus snake venom (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia cells mostly via oxidative stress-dependent signaling mechanism.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
L-amino acid oxidase isolated from Micrurus mipartitus snake venom (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia cells mostly via oxidative stress-dependent signaling mechanism.
Pulmonary Edema
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Stomach Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Thrombocytopenia
Comparative proteomes, immunoreactivities and neutralization of procoagulant activities of Calloselasma rhodostoma (Malayan pit viper) venoms from four regions in Southeast Asia.
Unconsciousness
Danger in the Canopy. Comparative Proteomics and Bioactivities of the Venoms of the South American Palm Pit Viper Bothrops bilineatus Subspecies bilineatus and smaragdinus and Antivenomics of B. b. bilineatus (Rondônia) Venom against the Brazilian Pentabothropic Antivenom.
Urolithiasis
Experimental urolithiasis : Part II--a comparative kinetic study of glyoxalase I, glycolate oxidase, alkaline phosphatase & lactate dehydrogenase in the normal rat kidney & bladder & its alterations in urolithiasis.
Uterine Cervical Neoplasms
ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells.
Virus Diseases
Barley Stripe Mosaic Virus ?b Interacts with Glycolate Oxidase and Inhibits Peroxisomal ROS Production to Facilitate Virus Infection.
Vitamin B 6 Deficiency
Vitamin B6 deficiency as related to oxalate-synthesizing enzymes in growing rats.
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0.0007 - 0.0108
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0012
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0003 - 0.0054
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0095 - 0.0107
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
0.00427 - 427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
0.0006 - 0.0124
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
0.0005 - 0.0104
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
0.0002 - 0.0226
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
0.0011 - 0.00812
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
0.0017 - 0.0022
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
0.0007 - 0.0023
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
0.0013 - 0.0134
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
0.0004 - 0.0315
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
0.0003 - 0.0135
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
0.0003 - 0.00523
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
0.0013 - 0.0073
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
0.00912 - 0.0357
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
0.0003 - 0.00634
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.002 - 0.0113
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0004 - 0.0083
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0011 - 0.0051
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0267 - 0.048
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0003 - 0.0083
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0009 - 0.0088
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.003 - 0.0076
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0005 - 0.0062
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0002 - 0.00113
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.00095 - 0.0358
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0137 - 0.0196
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0008 - 11
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0032 - 0.0407
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0006 - 0.0339
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0007 - 0.00714
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.00135 - 0.0031
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
0.0091
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0009 - 0.0052
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0005 - 0.0205
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0002 - 0.0186
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0011 - 0.0032
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0003 - 0.0135
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0116 - 0.0217
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0003 - 0.0166
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0004 - 0.01125
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0009 - 0.0095
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0009 - 0.0054
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0052 - 0.0318
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.00091
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004 - 0.0022
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0008 - 0.0042
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
0.0005 - 0.0021
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
0.0011 - 0.0018
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
3.7
Mandelate
Homo sapiens
-
-
1.8
oxalate
Homo sapiens
-
-
0.0007
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0108
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0054
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0095
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0107
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0006
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0124
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0104
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0226
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00812
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0017
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0022
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0023
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0134
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0315
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0135
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00523
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0073
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00912
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0357
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00634
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.002
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0113
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0083
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0051
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0267
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.048
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0083
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0088
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.003
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0076
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0005
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0062
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00113
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00095
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0358
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0137
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0196
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
11
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0032
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0407
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0006
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0339
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0007
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00714
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00135
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0031
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0052
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0205
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0186
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0032
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0135
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0116
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0217
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0166
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.01125
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0095
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0054
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0052
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0318
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0022
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0042
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0021
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0018
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
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Jones, J.M.; Morrell, J.C.; Gould, S.J.
Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases
J. Biol. Chem.
275
12590-12597
2000
Homo sapiens, Rattus sp.
brenda
Iwamoto, K.; Ikawa, T.
A novel glycolate oxidase requiring flavin mononucleotide as the cofactor in the Prasinophycean alga Mesostigma viride
Plant Cell Physiol.
41
988-991
2000
Mesostigma viride
brenda
Ferjancic-Biagini, A.; Dupuis, L.; De Caro, J.; Puigserver, A.
Inhibitory effects of anions and active site amino acid sequence of chicken liver L-2-hydroxyacid oxidase A, a member of the FMN-dependent alpha-hydroxy acid oxidizing enzyme family
Biochimie
80
1047-1054
1998
Gallus gallus
brenda
Stenberg, K.; Lindqvist, Y.
Three-dimensional structures of glycolate oxidase with bound active-site inhibitors
Protein Sci.
6
1009-1015
1997
Spinacia oleracea
brenda
Payne, M.S.; Petrillo, K.L.; Gavagan, J.E.; DiCosimo, R.; Wagner, L.W.; Anton, D.L.
Engineering Pichia pastoris for biocatalysis: co-production of two active enzymes
Gene
194
179-182
1997
Spinacia oleracea
brenda
Belmouden, A.; Lederer, F.
The role of a beta barrel loop 4 extension in modulating the physical and functional properties of long-chain 2-hydroxy-acid oxidase isozymes
Eur. J. Biochem.
238
790-798
1996
Rattus sp.
brenda
Stenberg, K.; Lindqvist, Y.
High-level expression, purification, and crystallization of recombinant spinach glycolate oxidase in Escherichia coli
Protein Expr. Purif.
8
295-298
1996
Spinacia oleracea
brenda
Payne, M.S.; Petrillo, K.L.; Gavagan, J.E.; Wagner, L.W.; DiCosimo, R.; Anton, D.L.
High-level production of spinach glycolate oxidase in the methylotrophic yeast Pichia pastoris: engineering a biocatalyst
Gene
167
215-219
1995
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Nicotiana benthamiana (E1AXT8)
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Zabaleta, N.; Barberia, M.; Martin-Higueras, C.; Zapata-Linares, N.; Betancor, I.; Rodriguez, S.; Martinez-Turrillas, R.; Torella, L.; Vales, A.; Olaguee, C.; Vilas-Zornoza, A.; Castro-Labrador, L.; Lara-Astiaso, D.; Prosper, F.; Salido, E.; Gonzalez-Aseguinolaza, G.; Rodriguez-Madoz, J.R.
CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type I
Nat. Commun.
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5454
2018
Mus musculus (Q9WU19)
brenda
Ahammed, G.J.; Li, X.; Zhang, G.; Zhang, H.; Shi, J.; Pan, C.; Yu, J.; Shi, K.
Tomato photorespiratory glycolate-oxidase-derived H2O2 production contributes to basal defence against Pseudomonas syringae
Plant Cell Environ.
41
1126-1138
2018
Solanum lycopersicum
brenda
Schmitz, J.; Huedig, M.; Meier, D.; Linka, N.; Maurino, V.G.
The genome of Ricinus communis encodes a single glycolate oxidase with different functions in photosynthetic and heterotrophic organs
Planta
252
100
2020
Ricinus communis (B9S0Y9), Ricinus communis (B9ST74), Ricinus communis
brenda
Xu, Y.P.; Yang, J.; Cai, X.Z.
Glycolate oxidase gene family in Nicotiana benthamiana genome-wide identification and functional analyses in disease resistance
Sci. Rep.
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8615
2018
Nicotiana benthamiana
brenda