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(2E)-3-phenylprop-2-en-1-ol + O2
(2E)-3-phenylprop-2-enal + H2O2
-
-
-
?
(2E)-hept-2-en-1-ol + O2
(2E)-hept-2-enal + H2O2
31.9% of the activity with benzyl alcohol
-
-
?
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
(2E,4E)-hepta-2,4-dien-1-ol + O2
(2E,4E)-hepta-2,4-dienal + H2O2
737% of the activity with benzyl alcohol
-
-
?
(2E,4E)-hexa-2,4-dien-1-ol + O2
(2E,4E)-hexa-2,4-dienal + H2O2
807% of the activity with benzyl alcohol
-
-
?
(2E,4E)-hexa-2,4-dien-1-ol + O2
? + H2O2
282% of the activity with benzyl alcohol
-
-
?
(2H-1,3-benzodioxol-5-yl)methanol + O2
2H-1,3-benzodioxole-5-carbaldehyde + H2O2
301% of the activity with benzyl alcohol
-
-
?
(2R,3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-ol + O2
(3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one + H2O2
4% conversion, 2% enantiomeric excess
-
-
?
(2R,3E)-4-(4-chlorophenyl)but-3-en-2-ol + O2
(3E)-4-(4-chlorophenyl)but-3-en-2-one + H2O2
10% conversion, 10% enantiomeric excess
-
-
?
(2R,3E)-4-(4-methylphenyl)but-3-en-2-ol + O2
(3E)-4-(4-methylphenyl)but-3-en-2-one + H2O2
13% conversion, 14% enantiomeric excess
-
-
?
(2R,3E)-4-phenylbut-3-en-2-ol + O2
(3E)-4-phenylbut-3-en-2-one + H2O2
29% conversion, 25% enantiomeric excess
-
-
?
(2R,3E)-oct-3-en-2-ol + O2
(3E)-oct-3-en-2-one + H2O2
16% conversion, 19% enantiomeric excess
-
-
?
(naphthalen-2-yl)methanol + O2
naphthalene-2-carbaldehyde + H2O2
874% of the activity with benzyl alcohol
-
-
?
(pyrene-1-yl)methanol + O2
pyrene-1-carbaldehyde + H2O2
35% of the activity with benzyl alcohol
-
-
?
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
(S)-1-(4-methoxyphenyl)-ethanol + O2
1-(4-methoxyphenyl)acetaldehyde + H2O2
-
-
-
?
(thiophen-2-yl)methanol + O2
thiophene-2-carbaldehyde + H2O2
15.8% of the activity with benzyl alcohol
-
-
?
1,1'-binaphthalene + O2
?
1,2,3,4,5-pentachlorobenzene + O2
?
1,2,3,4-tetrachlorobenzene + O2
?
1,2,4,5-tetrachlorobenzene + O2
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
1-amino-9,10-anthracenedione + O2
?
1-chloro-9,10-anthracenedione + O2
?
1-naphthalene methanol + O2
alpha-naphthaldehyde + H2O2
-
27% of the activity with cinnamyl alcohol
-
-
?
2,4-dichloroaniline + O2
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
2,4-hexadien-1-ol + 2 O2
2,4-hexadienal + 2 H2O2
-
-
-
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
2,4-hexadien-1-ol + O2
2,4-hexandienal + H2O2
-
-
-
-
?
2,4-hexadien-1-ol + O2
?
-
-
-
?
2,4-hexadien-1-ol + O2
? + H2O2
2,4-hexadienal + O2
2,4-hexadienoate + H2O2
-
-
-
?
2,5-diformylfuran + 2 O2
2,5-furandicarboxylic acid + H2O2
-
-
-
ir
2,5-diformylfuran + O2
5-formylfuran-2-carboxylic acid + ?
2,5-diformylfuran + O2
formylfurancarboxylic acid + ?
2,6-dichloroaniline + O2
?
2-anisyl alcohol + O2
2-anisyl aldehyde + H2O2
96% of the activity with benzyl alcohol
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
2-methoxybenzyl alcohol + O2
2-methoxybenzaldehyde + H2O
-
23% of the activity with 2-hydroxybenzyl alcohol
-
?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
2-naphthalenemethanol + O2
2-naphthaleneformaldehyde + H2O
-
745.7% of the activity with benzyl alcohol
-
?
2-naphthalenemethanol + O2
?
-
-
-
-
?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
3,4-difluorobenzaldehyde + O2
3,4-difluorobenzoic acid + H2O2
-
-
-
?, r
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
3,5-dimethoxybenzyl alcohol + O2
3,5-dimethoxy benzaldehyde + H2O2
-
7% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 8% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
3-anisyl alcohol + O2
3-anisaldehyde + H2O2
-
-
-
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
3-chloro-4-anisaldehyde + O2
3-chloro-4-anisic acid + H2O2
-
-
-
r
3-chloro-4-anisyl alcohol + O2
3-chloro-4-anisaldehyde + H2O2
-
-
-
?
3-chloro-4-anisyl alcohol + O2
3-chloro-4-anisyl aldehyde + H2O2
-
high activity
-
-
?
3-chloro-4-methoxybenzyl alcohol + O2
3-chloro-4-methoxybenzaldehyde + H2O2
ternary mechanism
-
-
?
3-chlorobenzaldehyde + O2
3-chlorobenzoic acid + H2O2
-
-
-
r
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
3-chlorobenzyl alcohol + O2
3-chlorobenzyl aldehyde + H2O2
-
-
-
-
?
3-fluorobenzaldehyde + O2
3-fluorobenzoic acid + H2O2
-
-
-
r
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
3-fluorobenzyl alcohol + O2
3-fluorobenzyl aldehyde + H2O2
-
low activity
-
-
?
3-fluorobenzyl alcohol + O2
?
-
-
-
?
3-hydroxy-4-methoxybenzyl alcohol + O2
3-hydroxy-4-methoxybenzaldehyde + H2O2
-
62% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 71% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
3-hydroxybenzyl alcohol + O2
3-hydroxybenzaldehyde + H2O2
3-hydroxybenzyl alcohol + O2
3-hydroxybenzyl aldehyde + H2O2
221% of the activity with benzyl alcohol
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
3-methoxybenzyl alcohol + O2
3-methoxybenzylaldehyde + H2O2
recombinant enzyme shows 1% of the activity with 2-hydroxybenzyl alcohol
-
-
?
3-phenoxybenzyl alcohol + O2
3-phenoxybenzaldehyde + H2O2
-
35% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 18% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
4-aminobenzyl alcohol + O2
4-aminobenzaldehyde + H2O2
18.6% of the activity with benzyl alcohol
-
-
?
4-anisaldehyde + O2
4-anisic acid + H2O2
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
4-chlorobenzaldehyde + O2
4-chlorobenzoic acid + H2O2
-
-
-
r
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
4-chlorobenzyl alcohol + O2
4-chlorobenzyl aldehyde + H2O2
-
-
-
-
?
4-fluorobenzaldehyde + O2
4-fluorobenzoic acid + H2O2
-
-
-
r
4-fluorobenzyl alcohol + O2
4-fluorobenzaldehyde + H2O2
-
-
-
?
4-fluorobenzyl alcohol + O2
4-fluorobenzyl aldehyde + H2O2
-
-
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
4-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
4-methoxybenzyl alcohol + O2
4-methoxybenzyl aldehyde + H2O2
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
-
-
-
r
4-nitrobenzaldehyde + O2
4-nitrobenzoic acid + H2O2
-
-
-
?, r
4-nitrobenzyl alcohol + O2
4-nitrobenzaldehyde + H2O2
-
-
-
r
5-(hydroxymethyl)furan-2-carboxylic acid + O2
2,5-formylfurancarboxylic acid + H2O2
-
-
-
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
2,5-furandicarboxylic acid + ?
very low activity
-
-
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
furan-2,5-dicarboxylic acid + ?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
5-hydroxymethylfurfural + O2
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
5-hydroxymethylfurfural + O2
2,5-furandicarboxylic acid + ?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
7H-benz[DE]anthracen-7-one + O2
?
9,10-anthracenedione + O2
?
anisyl alcohol + O2
anisaldehyde + H2O2
anisyl alcohol + O2
anisyl aldehyde + H2O2
benzaldehyde + O2
benzoic acid + H2O2
-
-
-
r
benzyl alcohol + O2
benzaldehyde + H2O2
benzyl alcohol + O2
benzyl aldehyde + H2O2
beta-naphthylcarbinol + O2
beta-naphthaldehyde + H2O2
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
cinnamyl alcohol + O2
cinnamic aldehyde + H2O2
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
coniferyl alcohol + O2
coniferyl aldehyde + H2O2
-
13% of the activity with cinnamyl alcohol
-
-
?
cumic alcohol + O2
cumic aldehyde + H2O2
149% of the activity with benzyl alcohol
-
-
?
cyclohexyl alcohol + O2
cyclohexyl aldehyde + H2O2
-
12% of the activity with cinnamyl alcohol
-
-
?
Direct Red 5B + O2
3-diazenyl-7-[(phenylcarbonyl)amino]naphthalene-2-sulfonic acid + H2O2
-
degradation, dye decolorizing
product identification by GC-MS analysis
-
?
ethanol + O2
acetaldehyde + H2O2
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
m-anisyl alcohol + O2
m-anisaldehyde + H2O2
N-phenyl-1-naphthalenamine + O2
?
n-propanol + O2
propionaldehyde + H2O2
vanillyl alcohol + O2
vanillyl aldehyde + H2O2
-
-
-
?
veratraldehyde + O2
veratric acid + H2O2
-
-
-
r
veratryl alcohol + 2,6-dichlorophenol indophenol
veratrylaldehyde + red. 2,6-dichlorophenol indophenol
-
-
-
-
?
veratryl alcohol + O2
? + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
veratryl alcohol + O2
veratryl aldehyde + H2O2
veratryl alcohol + O2
veratrylaldehyde + H2O2
additional information
?
-
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
-
-
-
?
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
63.9% of the activity with benzyl alcohol
-
-
?
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
-
-
-
-
?
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
over 98% excess of the R enantiomer after treatment of racemic 1-(4-methoxyphenyl)ethanol, the hydride transfer is highly stereoselective
-
-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
-
-
-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
mutant F501A
-
-
?
1,1'-binaphthalene + O2
?
-
low activity
-
-
?
1,1'-binaphthalene + O2
?
-
degradation, partial removal from soil
-
-
?
1,2,3,4,5-pentachlorobenzene + O2
?
-
very low activity
-
-
?
1,2,3,4,5-pentachlorobenzene + O2
?
-
degradation, partial removal from soil
-
-
?
1,2,3,4-tetrachlorobenzene + O2
?
-
high activity
-
-
?
1,2,3,4-tetrachlorobenzene + O2
?
-
degradation, complete removal from soil
-
-
?
1,2,4,5-tetrachlorobenzene + O2
?
-
high activity
-
-
?
1,2,4,5-tetrachlorobenzene + O2
?
-
degradation, complete removal from soil
-
-
?
1,2-binaphthalene + O2
?
-
low activity
-
-
?
1,2-binaphthalene + O2
?
-
degradation, partial removal from soil
-
-
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
-
-
-
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
degradation, partial removal from soil
-
-
?
1-amino-9,10-anthracenedione + O2
?
-
lower activity
-
-
?
1-amino-9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
1-chloro-9,10-anthracenedione + O2
?
-
very low activity
-
-
?
1-chloro-9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
2,4-dichloroaniline + O2
?
-
high activity
-
-
?
2,4-dichloroaniline + O2
?
-
degradation, complete removal from soil
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
-
-
r
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
177.5% of the activity with benzyl alcohol
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
-
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
286% of the activity with benzyl alcohol
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
-
50% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 75% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
-
-
-
-
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
-
-
-
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
-
high activity
-
-
?
2,4-hexadien-1-ol + O2
? + H2O2
-
531% of the activity with benzyl alcohol
-
?
2,4-hexadien-1-ol + O2
? + H2O2
-
-
-
-
?
2,5-diformylfuran + O2
5-formylfuran-2-carboxylic acid + ?
-
-
-
?
2,5-diformylfuran + O2
5-formylfuran-2-carboxylic acid + ?
-
-
-
?
2,5-diformylfuran + O2
formylfurancarboxylic acid + ?
-
-
-
?
2,5-diformylfuran + O2
formylfurancarboxylic acid + ?
-
-
-
-
?
2,6-dichloroaniline + O2
?
-
high activity
-
-
?
2,6-dichloroaniline + O2
?
-
degradation, complete removal from soil
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
-
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
-
i.e. salicyl alcohol
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
i.e. salicyl alcohol
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
-
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
i.e. salicyl alcohol
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
-
i.e. salicyl alcohol
-
?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
-
14% of the activity with 2-hydroxybenzyl alcohol
-
?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
recombinant enzyme shows 3.2% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 14% of the activity with 2-hydroxybenzyl alcohol
-
-
?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
recombinant enzyme shows 2.3% of the activity with 2-hydroxybenzyl alcohol
-
-
?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
-
21% of the activity with 2-hydroxybenzyl alcohol
-
?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
recombinant enzyme shows 19.1% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 21% of the activity with 2-hydroxybenzyl alcohol
-
-
?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
recombinant enzyme shows 21.9% of the activity with 2-hydroxybenzyl alcohol
-
-
?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
-
-
-
r
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
-
-
r
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
-
21% of the activity with 2-hydroxybenzyl alcohol
-
?
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
recombinant enzyme shows 3.8% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 21% of the activity with 2-hydroxybenzyl alcohol
-
-
?
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
recombinant enzyme shows 1.2% of the activity with 2-hydroxybenzyl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
i.e. veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
i.e. veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
-
326.1% of the activity with benzyl alcohol
-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
ternary mechanism
-
-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
-
5.6% of the activity with 4-methoxybenzyl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
31% of the activity with cinnamyl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
7.6% of the activity with anisyl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
at 63% of the activity with 3-methoxybenzyl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
-
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
297% of the activity with benzyl alcohol
-
-
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
-
-
-
-
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
-
-
-
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
-
-
-
-
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
-
-
-
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
ping-pong mechanism
-
-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
-
-
-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
ping-pong mechanism
-
-
?
3-hydroxybenzyl alcohol + O2
3-hydroxybenzaldehyde + H2O2
recombinant enzyme shows 13.1% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows less than 10% of the activity with 2-hydroxybenzyl alcohol
-
-
?
3-hydroxybenzyl alcohol + O2
3-hydroxybenzaldehyde + H2O2
recombinant enzyme shows 16.2% of the activity with 2-hydroxybenzyl alcohol
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
60% of the activity with cinnamyl alcohol
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
i.e. 3-anisyl alcohol
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
i.e. 3-anisyl alcohol
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
19% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 16% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
r
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
as active as benzyl alcohol
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
32% of the activity with 4-methoxybenzyl alcohol
-
-
?
4-anisaldehyde + O2
4-anisic acid + H2O2
-
-
-
?
4-anisaldehyde + O2
4-anisic acid + H2O2
-
-
-
-
?
4-anisaldehyde + O2
4-anisic acid + H2O2
-
-
-
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
-
-
-
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
best substrate
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
-
-
-
r
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
298% of the activity with benzyl alcohol
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
-
-
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
-
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
-
-
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
-
best substrate
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
-
-
-
?
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
-
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
15% of the activity with anisyl alcohol
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
r
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
12% of the activity with 4-methoxybenzyl alcohol
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
recombinant enzyme shows 2.7% of the activity with 2-hydroxybenzyl alcohol
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
-
-
r
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
-
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
-
7.6% of the activity with anisyl alcohol
-
-
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
207% of the activity with benzyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
63% of the activity with cinnamyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol, best substrate
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol, best substrate
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
200% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 266% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
15% of the activity with 3-methoxybenzyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
571.4% of the activity with benzyl alcohol
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
high activity, 4-methoxybenzyl alcohol, is one of the best substrates of AAO, and 4-methoxybenzaldehyde (4-anisaldehyde) is the main extracellular aromatic metabolite in Pleurotus species
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
ternary mechanism
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzyl aldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzyl aldehyde + H2O2
-
-
-
-
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
furan-2,5-dicarboxylic acid + ?
-
-
-
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
furan-2,5-dicarboxylic acid + ?
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
-
?
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
-
-
?
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
-
-
-
?
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-furandicarboxylic acid + ?
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-furandicarboxylic acid + ?
-
-
-
-
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
-
-
?
7H-benz[DE]anthracen-7-one + O2
?
-
low activity
-
-
?
7H-benz[DE]anthracen-7-one + O2
?
-
degradation, partial removal from soil
-
-
?
9,10-anthracenedione + O2
?
-
low activity
-
-
?
9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
anisyl alcohol + O2
anisaldehyde + H2O2
-
-
-
-
?
anisyl alcohol + O2
anisaldehyde + H2O2
-
-
-
-
?
anisyl alcohol + O2
anisaldehyde + H2O2
best substrate
-
-
?
anisyl alcohol + O2
anisaldehyde + H2O2
best substrate
-
-
?
anisyl alcohol + O2
anisaldehyde + H2O2
-
best substrate
-
-
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
647% of the activity with benzyl alcohol
-
-
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
-
-
-
-
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
-
-
-
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
26% of the activity with cinnamyl alcohol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
poorest substrate
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
poorest substrate
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
5.0% of the activity with anisyl alcohol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
recombinant enzyme shows 12.2% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 23% of the activity with 2-hydroxybenzyl alcohol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
recombinant enzyme shows 23.2% of the activity with 2-hydroxybenzyl alcohol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
30% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 25% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
19% conversion
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
at 28% of the activity with 3-methoxybenzyl alcohol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, overview
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
3.6% of the activity with 4-methoxybenzyl alcohol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzyl aldehyde + H2O2
-
-
-
?
benzyl alcohol + O2
benzyl aldehyde + H2O2
-
-
-
?
beta-naphthylcarbinol + O2
beta-naphthaldehyde + H2O2
-
80% of the activity with cinnamyl alcohol
-
-
?
beta-naphthylcarbinol + O2
beta-naphthaldehyde + H2O2
-
114% of the activity with 4-methoxybenzyl alcohol
-
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
-
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
-
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
-
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
-
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
-
-
r
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
high activity
-
-
r
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
451.1% of the activity with benzyl alcohol
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
-
-
-
?
cinnamyl alcohol + O2
cinnamic aldehyde + H2O2
-
-
-
-
?
cinnamyl alcohol + O2
cinnamic aldehyde + H2O2
-
oxidation at the gamma position, 77% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 55% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
289% of the activity with benzyl alcohol
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
-
-
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
442% of the activity with benzyl alcohol
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
-
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
-
-
-
?
diphenylether + O2
?
-
high activity
-
-
?
diphenylether + O2
?
-
degradation, complete removal from soil
-
-
?
diphenylsulfone + O2
?
-
low activity
-
-
?
diphenylsulfone + O2
?
-
degradation, partial removal from soil
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
low activity
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
low activity
-
-
?
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
?
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
-
?
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
-
-
?
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
-
-
-
?
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
-
-
-
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
73% of the activity with benzyl alcohol
-
-
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
-
-
-
-
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
246% of the activity with benzyl alcohol
-
-
?
m-anisyl alcohol + O2
m-anisaldehyde + H2O2
-
-
-
-
?
m-anisyl alcohol + O2
m-anisaldehyde + H2O2
-
-
-
-
?
N-phenyl-1-naphthalenamine + O2
?
-
high activity
-
-
?
N-phenyl-1-naphthalenamine + O2
?
-
degradation, complete removal from soil
-
-
?
n-propanol + O2
propionaldehyde + H2O2
-
-
-
-
?
n-propanol + O2
propionaldehyde + H2O2
-
-
-
-
?
naphthalene + O2
?
-
high activity
-
-
?
naphthalene + O2
?
-
degradation, complete removal from soil
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
r
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
318% of the activity with benzyl alcohol
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
322% of the activity with benzyl alcohol
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Pleurotus laciniatocrenatus
-
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
i.e. 3,4-dimethoxybenzyl alcohol
-
-
?
additional information
?
-
-
bifunctional enzyme showing aryl alcohol oxidase activity as well as secondary alcohol oxidase activity, EC 1.1.3.18, substrate specificity, overview
-
-
?
additional information
?
-
-
bifunctional enzyme showing aryl alcohol oxidase activity as well as secondary alcohol oxidase activity, EC 1.1.3.18, substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with 3,4-dimethoxyphenyl acetic acid and 1-(3,4-dimethoxyphenyl)-2-phenylethanol
-
-
?
additional information
?
-
-
ligninolytic activity
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds, extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
less than 10% of the activity with 2-hydroxybenzyl alcohol: 3-hydroxybenzyl alcohol, 3-methoxybenzyl alcohol. No activity with 4-hydroxybenzyl alcohol, 3-methylbenzylalcohol, 4-methylbenzyl alcohol, 4-methoxybenzyl alcohol. Traces of activity with 8-hydroxygeraniol
-
?
additional information
?
-
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
-
-
?
additional information
?
-
-
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
-
-
?
additional information
?
-
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
-
-
?
additional information
?
-
-
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
-
-
?
additional information
?
-
enzyme is active on short-chain alkane diols and glycerol, and aryl alcohols, with similar specific activity values. Highest specific activity is observed on 5-hydroxymethylfurfural. Galactose and galactosylated oligosaccharides are poor substrates
-
-
-
additional information
?
-
enzyme is active on short-chain alkane diols and glycerol, and aryl alcohols, with similar specific activity values. Highest specific activity is observed on 5-hydroxymethylfurfural. Galactose and galactosylated oligosaccharides are poor substrates
-
-
-
additional information
?
-
no activity with mono- and disaccharides. No electron acceptor: DCIP
-
-
-
additional information
?
-
-
no activity with mono- and disaccharides. No electron acceptor: DCIP
-
-
-
additional information
?
-
enzyme displays weak activity on carbohydrates
-
-
-
additional information
?
-
enzyme displays weak activity on carbohydrates
-
-
-
additional information
?
-
enzyme displays weak activity on carbohydrates
-
-
-
additional information
?
-
enzyme displays weak activity on carbohydrates
-
-
-
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
production of H2O2 during oxidation of lignin fragments
-
-
?
additional information
?
-
for sec-allylic alcohol substrates, exclusively oxidation of the allylic alcohol to the alpha,beta-unsaturated ketone is observed. The reaction is enantioselective for the R-enantiomer
-
-
-
additional information
?
-
-
ligninolytic activity
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
less than 10% of the activity with 2-hydroxybenzyl alcohol: 2-methylbenzyl alcohol, 3-hydroxybenzyl alcohol. No activity with benzyl alcohol, 4-hydroxybenzyl alcohol, 3-methylbenzylalcohol, 4-methylbenzyl alcohol, 4-methoxybenzyl alcohol. Traces of activity with 8-hydroxygeraniol, 2-phenylethyl alcohol, 3-methoxybenzyl alcohol
-
?
additional information
?
-
-
no activity with aliphatic and secondary aromatic alcohols
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
-
4-(hydroxymethyl)-benzoic acid is a poor substrate
-
-
?
additional information
?
-
-
an H2O2-producing ligninolytic enzyme, molecular docking study of substrates, overview
-
-
?
additional information
?
-
oxidation of aromatic and aliphatic polyunsaturated primary alcohols by wild-type and recombinant enzymes, overview
-
-
?
additional information
?
-
-
oxidation of aromatic and aliphatic polyunsaturated primary alcohols by wild-type and recombinant enzymes, overview
-
-
?
additional information
?
-
-
AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
-
-
?
additional information
?
-
-
during catalysis the non-covalently bound FAD cofactor is reduced by the substrate and subsequently reoxidized by molecular oxygen to yield hydrogen peroxide. The AAO substrate-binding pocket is located on the si side of the flavin ring and connected to the exposed surface by a hydrophobic substrate access channel. Two putative catalytic histidines, H502 and H546, are essential in AAO activity as a possible general bases in AAO catalysis. Residue F501, located near of cofactor and the putative catalytic histidines, is also involved in substrate oxidation by AAO
-
-
?
additional information
?
-
AAO typically oxidizes aromatic alcohols to the corresponding aldehydes. However, the enzyme can also oxidize aromatic aldehydes to the corresponding acids
-
-
?
additional information
?
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
substrate specificity, overview. AAO also shows some activity on aromatic aldehydes, the highest activity on 4-nitrobenzaldehyde being about 5% of the activity for benzyl alcohol. Extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids, AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds
-
-
?
additional information
?
-
-
substrate specificity, overview. AAO also shows some activity on aromatic aldehydes, the highest activity on 4-nitrobenzaldehyde being about 5% of the activity for benzyl alcohol. Extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids, AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds
-
-
?
additional information
?
-
the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid
-
-
?
additional information
?
-
the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
-
-
?
additional information
?
-
enzyme AAO is also able to oxidize some furanic compounds such as 5-hydroxymethylfurfural (HMF) and 2,5-diformylfuran (DFF), it has very low activity on 2,5-hydroxymethylfurancarboxylic acid, no activity with 2,5-formylfurancarboxylic acid. NMR analysis of the compounds
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity and highly stereoselective reaction mechanism. Assay method using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]/horseradish peroxidase
-
-
?
additional information
?
-
the enzyme shows a T-shaped stacking interaction between the Tyr92 side chain and the alcohol substrate at the catalytically competent position for concerted hydride and proton transfers. Bi-substrate kinetics analysis reveals that reactions with 3-chloro- or 3-fluorobenzyl alcohols (halogen substituents) proceed via a ping-pong mechanism. But mono- and dimethoxylated substituents (in 4-methoxybenzyl and 3,4-dimethoxybenzyl alcohols) alter the mechanism and a ternary complex is formed. Stacking energies, reaction mechanism, and kinetic analysis, role of Tyr92 in substrate binding and governing the kinetic mechanism in AAO, overview. Tyr-substrate binding energy and active site structure
-
-
?
additional information
?
-
for complete oxidation of 5-hydroxymethylfurfural, the rate-limiting step lies in the final oxidation of the intermediate 5-formyl-furancarboxylic acid to 2,5-furandicarboxylic acid. Wild-type AAO is not able to catalyze 5-formyl-furancarboxylic acid oxidation
-
-
-
additional information
?
-
Pleurotus laciniatocrenatus
-
a ligninolytic enzyme
-
-
?
additional information
?
-
-
ligninolytic activity
-
-
?
additional information
?
-
-
the enzyme participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
decolorization of coal humic acid by the extracellular enzyme produced by white-rot fungi, low activity, overview
-
-
?
additional information
?
-
-
degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil, e.g. from chemical industrial sites, overview
-
-
?
additional information
?
-
-
substrate specificity, lignin-modifying enzyme
-
-
?
additional information
?
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2. Addition of H2O2 instead of enzyme AAO leads to a faster degradation by the DyP enzyme in the first 4 min, but remains static afterwards for the rest of the incubation time
-
-
?
additional information
?
-
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2. Addition of H2O2 instead of enzyme AAO leads to a faster degradation by the DyP enzyme in the first 4 min, but remains static afterwards for the rest of the incubation time
-
-
?
additional information
?
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2. Addition of H2O2 instead of enzyme AAO leads to a faster degradation by the DyP enzyme in the first 4 min, but remains static afterwards for the rest of the incubation time
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
ligninolytic activity
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with caffeic acid
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with caffeic acid
-
-
?
additional information
?
-
no substrates: glucose, cellobiose, methanol
-
-
-
additional information
?
-
-
no substrates: glucose, cellobiose, methanol
-
-
-
additional information
?
-
no substrates: glucose, cellobiose, methanol
-
-
-
additional information
?
-
-
ligninolytic activity
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
-
-
?
additional information
?
-
-
the enzyme is able to oxidize several aromatic alcohols. Of the tested aryl-alcohols, the highest oxidation rate is obtained with 4-anisyl alcohol. Oxygen, 1,4-benzoquinone, and 2,6-dichloroindophenol can serve as electron acceptors. Assay method using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]/horseradish peroxidase. The enzyme shows no activity as a GMC oxidoreductase
-
-
?
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0.007 - 0.0164
(2E,4E)-hexa-2,4-dien-1-ol
0.0204 - 0.0382
(R,S)-4-methoxybenzyl alcohol
0.79 - 1.82
2,4-Dimethoxybenzyl alcohol
0.015 - 0.263
2,4-hexadien-1-ol
13
2,4-hexadienal
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
3.3 - 10
2,5-diformylfuran
28 - 132
2-hydroxybenzyl alcohol
3
3,4-difluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.39 - 2.88
3,4-dimethoxybenzyl alcohol
0.004 - 52.3
3-anisyl alcohol
0.7
3-chloro-4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.014
3-chloro-4-anisyl alcohol
-
pH 6.0, 24°C
1.5
3-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.107
3-Chlorobenzyl alcohol
-
pH 6.0, 24°C
2.2
3-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.554
3-fluorobenzyl alcohol
-
pH 6.0, 24°C
0.0057 - 0.301
3-Hydroxybenzyl alcohol
0.22 - 6.7
3-Methoxybenzyl alcohol
0.0076 - 88
4-anisyl alcohol
4.7
4-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.132
4-Chlorobenzyl alcohol
-
pH 6.0, 24°C
4.9
4-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.553
4-fluorobenzyl alcohol
-
pH 6.0, 24°C
0.042 - 19
4-Hydroxybenzyl alcohol
0.017 - 59
4-methoxybenzyl alcohol
2 - 5
4-nitrobenzaldehyde
3.1 - 42
5-(hydroxymethyl)furan-2-carboxylic acid
5.1 - 21.7
5-(hydroxymethyl)furfural
0.6 - 0.7
5-formylfuran-2-carboxylate
1.6 - 53
5-hydroxymethylfurfural
0.0048 - 1.03
anisyl alcohol
7
benzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.0012 - 86
benzyl alcohol
0.035 - 0.708
cinnamyl alcohol
4.8 - 38.9
furan-2,5-dicarbaldehyde
0.042 - 0.831
isovanillyl alcohol
0.22 - 0.3
m-anisyl alcohol
0.03
p-anisyl alcohol
-
recombinant enzyme
0.0063 - 0.98
Vanillyl alcohol
8
veratraldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.027 - 3.7
veratryl alcohol
additional information
additional information
-
0.007
(2E,4E)-hexa-2,4-dien-1-ol
mutant L416W, pH 7, 25°C
0.0156
(2E,4E)-hexa-2,4-dien-1-ol
wild-type, pH 7, 25°C
0.0164
(2E,4E)-hexa-2,4-dien-1-ol
mutant L416F, pH 7, 25°C
0.0204
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
0.0214
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C
0.0215
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)15(GGGGS)2, pH 4, 25°C
0.023
(R,S)-4-methoxybenzyl alcohol
-
free enzyme, pH 4, 25°C
0.028
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C
0.0382
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C
0.79
2,4-Dimethoxybenzyl alcohol
-
pH 6.0, 25°C
1.82
2,4-Dimethoxybenzyl alcohol
-
pH 6.0, 30°C
0.015
2,4-hexadien-1-ol
-
pH 6.0, 30°C
0.059
2,4-hexadien-1-ol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
0.081
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant F501Y
0.087
2,4-hexadien-1-ol
-
recombinant wild-type enzyme, pH 6.0, 24°C
0.091
2,4-hexadien-1-ol
25°C, pH 6.0, recombinant enzyme
0.092
2,4-hexadien-1-ol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.094
2,4-hexadien-1-ol
-
pH 6.0, 24°C
0.094
2,4-hexadien-1-ol
-
pH 6.0, 24°C, wild-type enzyme
0.095
2,4-hexadien-1-ol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.096
2,4-hexadien-1-ol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.106
2,4-hexadien-1-ol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
0.113
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant Y92F
0.114
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant L315A
0.12
2,4-hexadien-1-ol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.168
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant Y78A
0.263
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant F501A
3.3
2,5-diformylfuran
pH 6.0, 25°C
3.7
2,5-diformylfuran
pH 7.5, 25°C
10
2,5-diformylfuran
pH 7.5, 25°C
28
2-hydroxybenzyl alcohol
pH 6.0
40
2-hydroxybenzyl alcohol
pH 6.0
63
2-hydroxybenzyl alcohol
-
pH 6.0, 25°C
132
2-hydroxybenzyl alcohol
-
pH 6.0, 25°C
0.39
3,4-dimethoxybenzyl alcohol
-
-
0.41
3,4-dimethoxybenzyl alcohol
-
-
0.41
3,4-dimethoxybenzyl alcohol
-
enzyme form VAO I
0.41
3,4-dimethoxybenzyl alcohol
-
pH 6.0, 25°C
0.46
3,4-dimethoxybenzyl alcohol
-
enzyme form VAO II
0.56
3,4-dimethoxybenzyl alcohol
-
recombinant enzyme
1.2
3,4-dimethoxybenzyl alcohol
-
-
1.5
3,4-dimethoxybenzyl alcohol
-
-
2.88
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.004
3-anisyl alcohol
wild-type, pH 7, 25°C
0.031
3-anisyl alcohol
mutant L416W, pH 7, 25°C
0.034
3-anisyl alcohol
mutant L416F, pH 7, 25°C
0.211
3-anisyl alcohol
-
pH 6.0, 24°C, mutant L315A
0.215
3-anisyl alcohol
-
pH 6.0, 24°C, mutant F501Y
0.22
3-anisyl alcohol
pH 8.0, 25°C, wild-type enzyme
0.22
3-anisyl alcohol
native enzyme, pH 6, temperature not specified in the publication
0.227
3-anisyl alcohol
-
pH 6.0, 24°C
0.227
3-anisyl alcohol
-
pH 6.0, 24°C, wild-type enzyme
0.269
3-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.293
3-anisyl alcohol
-
pH 6.0, 24°C, mutant Y78A
0.293
3-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.3
3-anisyl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.301
3-anisyl alcohol
-
pH 6.0, 24°C, mutant Y92F
0.734
3-anisyl alcohol
-
pH 6.0, 24°C, mutant F501A
21
3-anisyl alcohol
wild-type, pH 7, 25°C
52.3
3-anisyl alcohol
mutant Y334F, pH 7, 25°C
0.0057
3-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
0.279
3-Hydroxybenzyl alcohol
mutant L416W, pH 7, 25°C
0.301
3-Hydroxybenzyl alcohol
mutant L416F, pH 7, 25°C
0.22
3-Methoxybenzyl alcohol
-
pH 6.0, 25°C
4.91
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
6.5
3-Methoxybenzyl alcohol
pH 7.5, 25°C
6.7
3-Methoxybenzyl alcohol
pH 7.5, 25°C
0.7
4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.8
4-anisaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.0076
4-anisyl alcohol
mutant L416W, pH 7, 25°C
0.012
4-anisyl alcohol
wild-type, pH 7, 25°C
0.015
4-anisyl alcohol
-
pH 6.0, 24°C, mutant F501Y
0.019
4-anisyl alcohol
mutant L416F, pH 7, 25°C
0.025
4-anisyl alcohol
25°C, pH 6.0, recombinant enzyme
0.026
4-anisyl alcohol
-
pH 6.0, 24°C, mutant F501A
0.027
4-anisyl alcohol
-
pH 6.0, 24°C
0.027
4-anisyl alcohol
-
pH 6.0, 24°C, wild-type enzyme
0.028
4-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.03
4-anisyl alcohol
-
-
0.03
4-anisyl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.037
4-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.039
4-anisyl alcohol
-
pH 6.0, 24°C, mutant Y92F
0.04
4-anisyl alcohol
-
-
0.04
4-anisyl alcohol
pH 8.0, 25°C, wild-type enzyme
0.04
4-anisyl alcohol
-
pH 6.0, 24°C, mutant L315A
0.04
4-anisyl alcohol
native enzyme, pH 6, temperature not specified in the publication
0.053
4-anisyl alcohol
-
pH 6.0, 24°C, mutant Y78A
24
4-anisyl alcohol
wild-type, pH 7, 25°C
88
4-anisyl alcohol
mutant Y334F, pH 7, 25°C
0.042
4-Hydroxybenzyl alcohol
-
pH 6.0, 30°C
0.0563
4-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
0.163
4-Hydroxybenzyl alcohol
mutant L416F, pH 7, 25°C
0.466
4-Hydroxybenzyl alcohol
mutant L416W, pH 7, 25°C
4.5
4-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
19
4-Hydroxybenzyl alcohol
mutant Y334F, pH 7, 25°C
0.017
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, overall reaction
0.022
4-methoxybenzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.023
4-methoxybenzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.025
4-methoxybenzyl alcohol
substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C
0.025
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant wild-type enzyme
0.028
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid
0.029
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, overall reaction
0.03
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92F
0.031
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 15 mM H2O2
0.0318
4-methoxybenzyl alcohol
pH 6, 25°C
0.0335
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 1 mM H2O2
0.034
4-methoxybenzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
0.035
4-methoxybenzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
0.037
4-methoxybenzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
0.038
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid
0.04
4-methoxybenzyl alcohol
-
pH 6.0, 25°C
0.046
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, oxidative half-reaction
0.048
4-methoxybenzyl alcohol
pH 60, 25°C, wild-type enzyme
0.049
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme
0.049
4-methoxybenzyl alcohol
substrate 4-methoxybenzyl alcohol, pH 6.0, 25°C
0.051
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92L
0.134
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, oxidative half-reaction
0.167
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
0.18
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, oxidative half-reaction
0.249
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
0.31
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H546A
0.31
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H546A
1.08
4-methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
1.16
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H546S
1.16
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H546S
1.289
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H502S
1.289
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H502S
1.3
4-methoxybenzyl alcohol
-
-
1.89
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92W
3.6
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, oxidative half-reaction
3.82
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H502A
3.82
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H502A
51
4-methoxybenzyl alcohol
pH 7.5, 25°C
59
4-methoxybenzyl alcohol
pH 7.5, 25°C
2
4-nitrobenzaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
5
4-nitrobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
3.1
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
4.4
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
26.9
5-(hydroxymethyl)furan-2-carboxylic acid
wild-type, pH 7, 25°C
27
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334F, pH 7, 25°C
42
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334W, pH 7, 25°C
5.1
5-(hydroxymethyl)furfural
-
pH 7, 25°C
9.1
5-(hydroxymethyl)furfural
pH 7, 25°C
21.7
5-(hydroxymethyl)furfural
-
pH 7, 25°C
0.6
5-formylfuran-2-carboxylate
-
pH 7, 25°C
0.7
5-formylfuran-2-carboxylate
-
pH 7, 25°C
1.6
5-hydroxymethylfurfural
pH 6.0, 25°C
1.6
5-hydroxymethylfurfural
wild-type, pH 6, 25°C
6.5
5-hydroxymethylfurfural
wild-type, pH 7, 25°C
12.4
5-hydroxymethylfurfural
mutant H91N/L170M/F501W, pH 6, 25°C
13
5-hydroxymethylfurfural
mutant H91N/L170M, pH 6, 25°C
13.02
5-hydroxymethylfurfural
pH 6, 30°C
14
5-hydroxymethylfurfural
pH 7.5, 25°C
14
5-hydroxymethylfurfural
mutant Y334F, pH 7, 25°C
17
5-hydroxymethylfurfural
pH 7.5, 25°C
53
5-hydroxymethylfurfural
mutant Y334W, pH 7, 25°C
0.0048
anisyl alcohol
-
pH 6.0, 30°C
0.059
anisyl alcohol
pH 6.0, 30°C
0.108
anisyl alcohol
-
mutant F501A expressed in Emericella nidulans
0.12
anisyl alcohol
-
mutant F501Y expressed in Emericella nidulans
0.794
anisyl alcohol
-
wild-type enzyme expressed in Escherichia coli
0.836
anisyl alcohol
-
wild-type enzyme expressed in Emericella nidulans
1.03
anisyl alcohol
pH 6, 30°C
0.0012
benzyl alcohol
wild-type, pH 7, 25°C
0.0059
benzyl alcohol
mutant L416W, pH 7, 25°C
0.0079
benzyl alcohol
mutant L416F, pH 7, 25°C
0.03
benzyl alcohol
-
pH 8.0, 30°C
0.051
benzyl alcohol
-
mutant F501A expressed in Emericella nidulans
0.189
benzyl alcohol
-
mutant F501Y expressed in Emericella nidulans
0.37
benzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.38
benzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.388
benzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
0.39
benzyl alcohol
-
wild-type enzyme expressed in Escherichia coli
0.44
benzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
0.504
benzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
0.614
benzyl alcohol
-
pH 6.0, 24°C, mutant F501Y
0.63
benzyl alcohol
-
recombinant enzyme
0.63
benzyl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.632
benzyl alcohol
-
pH 6.0, 24°C
0.632
benzyl alcohol
-
pH 6.0, 24°C, wild-type enzyme
0.639
benzyl alcohol
-
pH 6.0, 24°C, mutant Y78A
0.719
benzyl alcohol
-
pH 6.0, 24°C, mutant L315A
0.758
benzyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.784
benzyl alcohol
pH 6.0, 30°C
0.84
benzyl alcohol
-
pH 6.0, 25°C
0.84
benzyl alcohol
pH 8.0, 25°C, wild-type enzyme
0.85
benzyl alcohol
native enzyme, pH 6, temperature not specified in the publication
0.873
benzyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.947
benzyl alcohol
-
wild-type enzyme expressed in Emericella nidulans
0.985
benzyl alcohol
-
pH 6.0, 24°C, mutant Y92F
2.5 - 5
benzyl alcohol
-
pH 6.0, 24°C, mutant F501A
10.8
benzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
27
benzyl alcohol
wild-type, pH 7, 25°C
30
benzyl alcohol
pH 7.5, 25°C
61
benzyl alcohol
mutant Y334F, pH 7, 25°C
86
benzyl alcohol
pH 7.5, 25°C
0.035
cinnamyl alcohol
-
pH 6.0, 30°C
0.49
cinnamyl alcohol
pH 6, 30°C
0.708
cinnamyl alcohol
-
pH 6.0, 24°C
4.8
furan-2,5-dicarbaldehyde
-
pH 7, 25°C
6.8
furan-2,5-dicarbaldehyde
pH 7, 25°C
38.9
furan-2,5-dicarbaldehyde
-
pH 7, 25°C
0.042
isovanillyl alcohol
wild-type, pH 7, 25°C
0.154
isovanillyl alcohol
mutant L416W, pH 7, 25°C
0.318
isovanillyl alcohol
mutant L416F, pH 7, 25°C
0.831
isovanillyl alcohol
-
pH 6.0, 24°C
0.22
m-anisyl alcohol
-
-
0.22
m-anisyl alcohol
-
-
0.3
m-anisyl alcohol
-
recombinant enzyme
0.017
O2
with 3-fluorobenzyl alcohol, 25°C, pH 6.0, recombinant enzyme
0.232
O2
with 2,4-hexadien-1-ol, 25°C, pH 6.0, recombinant enzyme
0.348
O2
with 4-anisyl alcohol, 25°C, pH 6.0, recombinant enzyme
0.0063
Vanillyl alcohol
wild-type, pH 7, 25°C
0.025
Vanillyl alcohol
-
-
0.419
Vanillyl alcohol
mutant L416W, pH 7, 25°C
0.98
Vanillyl alcohol
mutant L416F, pH 7, 25°C
0.027
veratryl alcohol
-
wild-type enzyme expressed in Emericella nidulans
0.044
veratryl alcohol
-
mutant F501A expressed in Emericella nidulans
0.0483
veratryl alcohol
wild-type, pH 7, 25°C
0.05
veratryl alcohol
-
wild-type enzyme expressed in Escherichia coli
0.12
veratryl alcohol
-
pH 6.0, 30°C
0.123
veratryl alcohol
-
mutant F501Y expressed in Emericella nidulans
0.317
veratryl alcohol
-
pH 6.0, 24°C, mutant F501Y
0.34
veratryl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.36
veratryl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.38
veratryl alcohol
-
pH 6.0, 24°C, mutant F501A
0.41
veratryl alcohol
pH 8.0, 25°C, wild-type enzyme
0.41
veratryl alcohol
native enzyme, pH 6, temperature not specified in the publication
0.41
veratryl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
0.424
veratryl alcohol
mutant L416F, pH 7, 25°C
0.46
veratryl alcohol
-
pH 6.0, 24°C, mutant Y92F
0.47
veratryl alcohol
pH 6, 30°C
0.49 - 2
veratryl alcohol
-
pH 6.0, 24°C, mutant Y78A
0.51
veratryl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
0.529
veratryl alcohol
pH 6.0, 30°C
0.54
veratryl alcohol
-
pH 6.0, 24°C
0.54
veratryl alcohol
-
pH 6.0, 24°C, wild-type enzyme
0.541
veratryl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.56
veratryl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.59 - 1
veratryl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.6
veratryl alcohol
-
pH 6.0, 40°C
0.686
veratryl alcohol
mutant L416W, pH 7, 25°C
0.77
veratryl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
0.844
veratryl alcohol
-
pH 6.0, 24°C, mutant L315A
1.162
veratryl alcohol
-
pH 3.0, 40°C
3
veratryl alcohol
pH 7.5, 25°C
3.7
veratryl alcohol
pH 7.5, 25°C
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
stopped-flow and steady-state kinetics
-
additional information
additional information
-
MichaelisMenten kinetics and redox potentials of wild-type and mutant enzymes, overview
-
additional information
additional information
steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview
-
additional information
additional information
mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base
-
additional information
additional information
-
mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base
-
additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of overall and half-reactions of wild-type and mutant enzymes by (anaerobic) stopped-flow spectrophotometry, changes in the flavin redox state, detailed overview
-
additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady state and transient state kinetic constants for alcohol and O2 of AAO oxidation of a deuterated and normal (alpha-protiated) 4-methoxybenzyl alcohol, solvent kinetic isotope effects, overview
-
additional information
additional information
steady-state and transient kinetics of overall reaction, and oxidative and reductive half-reactions, overview
-
additional information
additional information
steady-state and stopped-flow kinetics, bi-substrate kinetics analysis, kinetic mechanisms, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
17.3 - 68.4
(2E,4E)-hexa-2,4-dien-1-ol
29 - 44
(R,S)-4-methoxybenzyl alcohol
30
2,4-Dimethoxybenzyl alcohol
-
pH 6.0, 30°C
1 - 206
2,4-hexadien-1-ol
0.33
2,4-hexadienal
wild type enzyme, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
1.4 - 31.4
2,5-diformylfuran
0.867
3,4-difluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
30 - 105.7
3,4-dimethoxybenzyl alcohol
0.057
3-chloro-4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
46
3-chloro-4-anisyl alcohol
-
pH 6.0, 24°C
0.85
3-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
22
3-Chlorobenzyl alcohol
-
pH 6.0, 24°C
0.883
3-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
6
3-fluorobenzyl alcohol
-
pH 6.0, 24°C
1.17 - 9.91
3-Hydroxybenzyl alcohol
34 - 115.4
3-Methoxybenzyl alcohol
0.012 - 0.12
4-anisaldehyde
1.05
4-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
51
4-Chlorobenzyl alcohol
-
pH 6.0, 24°C
0.367
4-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
32
4-fluorobenzyl alcohol
-
pH 6.0, 24°C
0.54 - 75
4-Hydroxybenzyl alcohol
0.069 - 208
4-methoxybenzyl alcohol
1.21 - 1.633
4-nitrobenzaldehyde
3.7 - 28.3
5-(hydroxymethyl)furan-2-carboxylic acid
0.24 - 1.38
5-(hydroxymethyl)furfural
0.002 - 0.008
5-formylfuran-2-carboxylate
0.0008 - 201
5-hydroxymethylfurfural
0.0075 - 203
anisyl alcohol
0.5
benzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.0069 - 88
cinnamyl alcohol
0.01 - 0.1
furan-2,5-dicarbaldehyde
2.05 - 127
isovanillyl alcohol
8.27
m-anisyl alcohol
-
-
48.5
p-anisyl alcohol
-
-
0.81 - 21.3
Vanillyl alcohol
0.13
veratraldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.0053 - 116
veratryl alcohol
17.3
(2E,4E)-hexa-2,4-dien-1-ol
mutant L416W, pH 7, 25°C
48.3
(2E,4E)-hexa-2,4-dien-1-ol
wild-type, pH 7, 25°C
68.4
(2E,4E)-hexa-2,4-dien-1-ol
mutant L416F, pH 7, 25°C
29
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C
30
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C
30
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C
34
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)15(GGGGS)2, pH 4, 25°C
41
(R,S)-4-methoxybenzyl alcohol
-
free enzyme, pH 4, 25°C
44
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
1
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant F501A
47
2,4-hexadien-1-ol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
52
2,4-hexadien-1-ol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
56
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant L315A
62
2,4-hexadien-1-ol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
64
2,4-hexadien-1-ol
-
pH 6.0, 30°C
89
2,4-hexadien-1-ol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
110
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant F501Y
119
2,4-hexadien-1-ol
-
pH 6.0, 24°C
119
2,4-hexadien-1-ol
-
pH 6.0, 24°C, wild-type enzyme
136
2,4-hexadien-1-ol
-
recombinant wild-type enzyme, pH 6.0, 24°C
161
2,4-hexadien-1-ol
25°C, pH 6.0, recombinant enzyme
177
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant Y78A
206
2,4-hexadien-1-ol
-
pH 6.0, 24°C, mutant Y92F
1.4
2,5-diformylfuran
pH 7.5, 25°C
3.6
2,5-diformylfuran
pH 7.5, 25°C
31.4
2,5-diformylfuran
pH 6.0, 25°C
30
3,4-dimethoxybenzyl alcohol
-
-
64.3
3,4-dimethoxybenzyl alcohol
-
enzyme form VAO II
82.2
3,4-dimethoxybenzyl alcohol
-
enzyme form VAO I
105.7
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
1
3-anisyl alcohol
-
pH 6.0, 24°C, mutant F501A
7.66
3-anisyl alcohol
wild-type, pH 7, 25°C
8
3-anisyl alcohol
-
pH 6.0, 24°C, mutant Y78A
11.3
3-anisyl alcohol
mutant L416W, pH 7, 25°C
12
3-anisyl alcohol
-
pH 6.0, 24°C, mutant L315A
12.4
3-anisyl alcohol
mutant L416F, pH 7, 25°C
15
3-anisyl alcohol
-
pH 6.0, 24°C
15
3-anisyl alcohol
-
pH 6.0, 24°C, wild-type enzyme
17
3-anisyl alcohol
-
pH 6.0, 24°C, mutant F501Y
26
3-anisyl alcohol
-
pH 6.0, 24°C, mutant Y92F
140
3-anisyl alcohol
wild-type, pH 7, 25°C
289
3-anisyl alcohol
mutant Y334F, pH 7, 25°C
1.17
3-Hydroxybenzyl alcohol
mutant L416W, pH 7, 25°C
7.5
3-Hydroxybenzyl alcohol
mutant L416F, pH 7, 25°C
9.91
3-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
34
3-Methoxybenzyl alcohol
pH 7.5, 25°C
52
3-Methoxybenzyl alcohol
pH 7.5, 25°C
115.4
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.012
4-anisaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.05
4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.11
4-anisaldehyde
pH 6, 25°C, presence of 1 mM H2O2
0.11
4-anisaldehyde
pH 6, 25°C, presence of 15 mM H2O2
0.12
4-anisaldehyde
pH 6, 25°C
3
4-anisyl alcohol
-
pH 6.0, 24°C, mutant F501A
3.49
4-anisyl alcohol
mutant L416W, pH 7, 25°C
12.5
4-anisyl alcohol
wild-type, pH 7, 25°C
14.2
4-anisyl alcohol
mutant L416F, pH 7, 25°C
48
4-anisyl alcohol
wild-type, pH 7, 25°C
60
4-anisyl alcohol
-
pH 6.0, 24°C, mutant L315A
90
4-anisyl alcohol
-
pH 6.0, 24°C, mutant Y78A
111
4-anisyl alcohol
-
pH 6.0, 24°C, mutant F501Y
129
4-anisyl alcohol
25°C, pH 6.0, recombinant enzyme
139
4-anisyl alcohol
-
pH 6.0, 24°C, mutant Y92F
142
4-anisyl alcohol
-
pH 6.0, 24°C
142
4-anisyl alcohol
-
pH 6.0, 24°C, wild-type enzyme
218
4-anisyl alcohol
mutant Y334F, pH 7, 25°C
0.54
4-Hydroxybenzyl alcohol
mutant L416W, pH 7, 25°C
4.81
4-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
8.77
4-Hydroxybenzyl alcohol
mutant L416F, pH 7, 25°C
20.1
4-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
33
4-Hydroxybenzyl alcohol
mutant Y334F, pH 7, 25°C
75
4-Hydroxybenzyl alcohol
-
pH 6.0, 30°C
0.069
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H502S
0.069
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H502S
0.072
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H502A
0.072
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H502A
1.03
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid
1.32
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid
3.5
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H546A
3.5
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H546A
11
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92W
17
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H546S
17
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H546S
25
4-methoxybenzyl alcohol
substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C
32
4-methoxybenzyl alcohol
pH 7.5, 25°C
34
4-methoxybenzyl alcohol
pH 7.5, 25°C
40
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
41
4-methoxybenzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
54
4-methoxybenzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
56.9
4-methoxybenzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
64
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
70
4-methoxybenzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
87
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, overall reaction
97
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 15 mM H2O2
100
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92L
104
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 1 mM H2O2
105
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, overall reaction
105
4-methoxybenzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
108
4-methoxybenzyl alcohol
pH 6, 25°C
120
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92F
129
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant wild-type enzyme
140.9
4-methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
196
4-methoxybenzyl alcohol
substrate 4-methoxybenzyl alcohol, pH 6.0, 25°C
197
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme
208
4-methoxybenzyl alcohol
pH 60, 25°C, wild-type enzyme
1.21
4-nitrobenzaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
1.633
4-nitrobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
3.7
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334W, pH 7, 25°C
3.8
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
5.2
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
15.4
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334F, pH 7, 25°C
28.3
5-(hydroxymethyl)furan-2-carboxylic acid
wild-type, pH 7, 25°C
0.24
5-(hydroxymethyl)furfural
-
pH 7, 25°C
1
5-(hydroxymethyl)furfural
-
pH 7, 25°C
1.38
5-(hydroxymethyl)furfural
pH 7, 25°C
0.002
5-formylfuran-2-carboxylate
-
pH 7, 25°C
0.008
5-formylfuran-2-carboxylate
-
pH 7, 25°C
0.0008
5-hydroxymethylfurfural
pH 6, 30°C
0.67
5-hydroxymethylfurfural
wild-type, pH 6, 25°C
6.8
5-hydroxymethylfurfural
mutant H91N/L170M, pH 6, 25°C
18.8
5-hydroxymethylfurfural
mutant H91N/L170M/F501W, pH 6, 25°C
20.1
5-hydroxymethylfurfural
pH 6.0, 25°C
26
5-hydroxymethylfurfural
pH 7.5, 25°C
29
5-hydroxymethylfurfural
pH 7.5, 25°C
71
5-hydroxymethylfurfural
mutant Y334W, pH 7, 25°C
126
5-hydroxymethylfurfural
wild-type, pH 7, 25°C
201
5-hydroxymethylfurfural
mutant Y334F, pH 7, 25°C
0.0075
anisyl alcohol
pH 6, 30°C
45
anisyl alcohol
-
pH 6.0, 30°C
203
anisyl alcohol
pH 6.0, 30°C
1
benzyl alcohol
-
pH 6.0, 24°C, mutant F501A
2.2
benzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
3.84
benzyl alcohol
mutant L416W, pH 7, 25°C
6.13
benzyl alcohol
wild-type, pH 7, 25°C
8.03
benzyl alcohol
mutant L416F, pH 7, 25°C
15.1
benzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
19
benzyl alcohol
-
pH 6.0, 24°C, mutant L315A
19
benzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
22
benzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
23.4
benzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
25
benzyl alcohol
-
pH 6.0, 24°C, mutant Y78A
27
benzyl alcohol
-
pH 6.0, 24°C, mutant F501Y
30
benzyl alcohol
-
pH 6.0, 24°C
30
benzyl alcohol
-
pH 6.0, 24°C, wild-type enzyme
31
benzyl alcohol
pH 7.5, 25°C
33
benzyl alcohol
-
pH 6.0, 24°C, mutant Y92F
34.4
benzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
37
benzyl alcohol
pH 7.5, 25°C
38
benzyl alcohol
pH 6.0, 30°C
54.5
benzyl alcohol
wild-type, pH 7, 25°C
226
benzyl alcohol
mutant Y334F, pH 7, 25°C
0.0069
cinnamyl alcohol
pH 6, 30°C
65
cinnamyl alcohol
-
pH 6.0, 24°C
88
cinnamyl alcohol
-
pH 6.0, 30°C
0.01
furan-2,5-dicarbaldehyde
-
pH 7, 25°C
0.017
furan-2,5-dicarbaldehyde
-
pH 7, 25°C
0.1
furan-2,5-dicarbaldehyde
pH 7, 25°C
2.05
isovanillyl alcohol
mutant L416W, pH 7, 25°C
7.02
isovanillyl alcohol
wild-type, pH 7, 25°C
8.67
isovanillyl alcohol
mutant L416F, pH 7, 25°C
127
isovanillyl alcohol
-
pH 6.0, 24°C
0.81
Vanillyl alcohol
mutant L416W, pH 7, 25°C
14.7
Vanillyl alcohol
wild-type, pH 7, 25°C
21.3
Vanillyl alcohol
mutant L416F, pH 7, 25°C
0.0053
veratryl alcohol
pH 6, 30°C
2 - 8
veratryl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
2.96
veratryl alcohol
mutant L416W, pH 7, 25°C
3
veratryl alcohol
-
pH 6.0, 24°C, mutant F501A
12.4
veratryl alcohol
mutant L416F, pH 7, 25°C
13.2
veratryl alcohol
wild-type, pH 7, 25°C
24.6
veratryl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
25
veratryl alcohol
pH 7.5, 25°C
36.8
veratryl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
41
veratryl alcohol
pH 7.5, 25°C
53
veratryl alcohol
-
pH 6.0, 30°C
56.9
veratryl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
66
veratryl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
70
veratryl alcohol
pH 6.0, 30°C
76
veratryl alcohol
-
pH 6.0, 24°C, mutant L315A
83
veratryl alcohol
-
pH 6.0, 24°C, mutant Y78A
86
veratryl alcohol
-
pH 6.0, 24°C, mutant F501Y
114
veratryl alcohol
-
pH 6.0, 24°C
114
veratryl alcohol
-
pH 6.0, 24°C, wild-type enzyme
116
veratryl alcohol
-
pH 6.0, 24°C, mutant Y92F
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2460 - 4180
(2E,4E)-hexa-2,4-dien-1-ol
747 - 2183
(R,S)-4-methoxybenzyl alcohol
16.5
2,4-Dimethoxybenzyl alcohol
-
pH 6.0, 30°C
456 - 4270
2,4-hexadien-1-ol
0.025
2,4-hexadienal
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.157 - 0.38
2,5-diformylfuran
0.282
3,4-difluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
39.7
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.85 - 1940
3-anisyl alcohol
0.085
3-chloro-4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.643
3-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.407
3-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
4.2 - 1750
3-Hydroxybenzyl alcohol
5.1 - 23.5
3-Methoxybenzyl alcohol
0.013 - 0.087
4-anisaldehyde
0.66 - 1080
4-anisyl alcohol
0.223
4-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.075
4-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.45 - 1790
4-Hydroxybenzyl alcohol
0.019 - 5160
4-methoxybenzyl alcohol
0.315 - 0.597
4-nitrobenzaldehyde
0.0167 - 1.7
5-(hydroxymethyl)furan-2-carboxylic acid
0.047 - 0.15
5-(hydroxymethyl)furfural
0.001 - 0.0023
5-formylfuran-2-carboxylate
0.001 - 19.4
5-hydroxymethylfurfural
0.008 - 9380
anisyl alcohol
0.073
benzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.2 - 5060
benzyl alcohol
0.014 - 2510
cinnamyl alcohol
0.0025 - 0.015
furan-2,5-dicarbaldehyde
13.3 - 167
isovanillyl alcohol
1.9 - 2350
Vanillyl alcohol
0.0167
veratraldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.011 - 440
veratryl alcohol
2460
(2E,4E)-hexa-2,4-dien-1-ol
mutant L416W, pH 7, 25°C
3100
(2E,4E)-hexa-2,4-dien-1-ol
wild-type, pH 7, 25°C
4180
(2E,4E)-hexa-2,4-dien-1-ol
mutant L416F, pH 7, 25°C
747
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C
1061
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C
1383
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C
1568
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)15(GGGGS)2, pH 4, 25°C
1782
(R,S)-4-methoxybenzyl alcohol
-
free enzyme, pH 4, 25°C
2183
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
456
2,4-hexadien-1-ol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
653
2,4-hexadien-1-ol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
840
2,4-hexadien-1-ol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
866
2,4-hexadien-1-ol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
1555
2,4-hexadien-1-ol
-
recombinant wild-type enzyme, pH 6.0, 24°C
4270
2,4-hexadien-1-ol
-
pH 6.0, 30°C
0.157
2,5-diformylfuran
pH 6.0, 25°C
0.36
2,5-diformylfuran
pH 7.5, 25°C
0.38
2,5-diformylfuran
pH 7.5, 25°C
0.85
3-anisyl alcohol
mutant Y334W, pH 7, 25°C
5.5
3-anisyl alcohol
mutant Y334F, pH 7, 25°C
6.6
3-anisyl alcohol
wild-type, pH 7, 25°C
361
3-anisyl alcohol
mutant L416F, pH 7, 25°C
367
3-anisyl alcohol
mutant L416W, pH 7, 25°C
1940
3-anisyl alcohol
wild-type, pH 7, 25°C
4.2
3-Hydroxybenzyl alcohol
mutant L416W, pH 7, 25°C
25
3-Hydroxybenzyl alcohol
mutant L416F, pH 7, 25°C
1750
3-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
5.1
3-Methoxybenzyl alcohol
pH 7.5, 25°C
8
3-Methoxybenzyl alcohol
pH 7.5, 25°C
23.5
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.013
4-anisaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.087
4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.66
4-anisyl alcohol
mutant Y334W, pH 7, 25°C
2
4-anisyl alcohol
wild-type, pH 7, 25°C
2.47
4-anisyl alcohol
mutant Y334F, pH 7, 25°C
461
4-anisyl alcohol
mutant L416W, pH 7, 25°C
740
4-anisyl alcohol
mutant L416F, pH 7, 25°C
1080
4-anisyl alcohol
wild-type, pH 7, 25°C
0.45
4-Hydroxybenzyl alcohol
mutant Y334W, pH 7, 25°C
1.2
4-Hydroxybenzyl alcohol
mutant L416W, pH 7, 25°C
1.74
4-Hydroxybenzyl alcohol
mutant Y334F, pH 7, 25°C
4.5
4-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
53.9
4-Hydroxybenzyl alcohol
mutant L416F, pH 7, 25°C
85.5
4-Hydroxybenzyl alcohol
wild-type, pH 7, 25°C
1790
4-Hydroxybenzyl alcohol
-
pH 6.0, 30°C
0.019
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H502S
0.019
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H502S
0.054
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H502A
0.054
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H502A
0.29
4-methoxybenzyl alcohol
pH 7.5, 25°C
0.54
4-methoxybenzyl alcohol
pH 7.5, 25°C
3
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H546S
3
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H546S
6
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92W
11
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, oxidative half-reaction
53
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant H546A
53
4-methoxybenzyl alcohol
pH 60, 25°C, mutant H546A
130.5
4-methoxybenzyl alcohol
at pH 6.0 and 30°C
240
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
257
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
483
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, oxidative half-reaction
784
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, oxidative half-reaction
1020
4-methoxybenzyl alcohol
substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C
1390
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, oxidative half-reaction
1562
4-methoxybenzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
1782
4-methoxybenzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
1909
4-methoxybenzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
1940
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92L
2080
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid
2250
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid
2586
4-methoxybenzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
2979
4-methoxybenzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
3100
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 1 mM H2O2
3120
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 15 mM H2O2
3390
4-methoxybenzyl alcohol
pH 6, 25°C
3620
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, overall reaction
3980
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme
3980
4-methoxybenzyl alcohol
substrate 4-methoxybenzyl alcohol, pH 6.0, 25°C
4330
4-methoxybenzyl alcohol
pH 60, 25°C, wild-type enzyme
4450
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92F
5120
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, overall reaction
5160
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant wild-type enzyme
0.315
4-nitrobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.597
4-nitrobenzaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.0167
5-(hydroxymethyl)furan-2-carboxylic acid
pH 6.0, 25°C
0.088
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334W, pH 7, 25°C
0.57
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334F, pH 7, 25°C
0.86
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
1.1
5-(hydroxymethyl)furan-2-carboxylic acid
wild-type, pH 7, 25°C
1.7
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
0.047
5-(hydroxymethyl)furfural
-
pH 7, 25°C
0.05
5-(hydroxymethyl)furfural
-
pH 7, 25°C
0.15
5-(hydroxymethyl)furfural
pH 7, 25°C
0.001
5-formylfuran-2-carboxylate
pH 7, 25°C
0.0015
5-formylfuran-2-carboxylate
-
pH 7, 25°C
0.0023
5-formylfuran-2-carboxylate
-
pH 7, 25°C
0.001
5-hydroxymethylfurfural
pH 6, 30°C
0.215
5-hydroxymethylfurfural
pH 6.0, 25°C
0.42
5-hydroxymethylfurfural
wild-type, pH 6, 25°C
0.52
5-hydroxymethylfurfural
mutant H91N/L170M, pH 6, 25°C
1.34
5-hydroxymethylfurfural
mutant Y334W, pH 7, 25°C
1.5
5-hydroxymethylfurfural
pH 7.5, 25°C
1.51
5-hydroxymethylfurfural
mutant H91N/L170M/F501W, pH 6, 25°C
2.1
5-hydroxymethylfurfural
pH 7.5, 25°C
14.4
5-hydroxymethylfurfural
mutant Y334F, pH 7, 25°C
19.4
5-hydroxymethylfurfural
wild-type, pH 7, 25°C
0.008
anisyl alcohol
pH 6, 30°C
3466
anisyl alcohol
pH 6.0, 30°C
9380
anisyl alcohol
-
pH 6.0, 30°C
0.2
benzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.43
benzyl alcohol
pH 7.5, 25°C
0.75
benzyl alcohol
mutant Y334W, pH 7, 25°C
1
benzyl alcohol
pH 7.5, 25°C
2
benzyl alcohol
wild-type, pH 7, 25°C
3.7
benzyl alcohol
mutant Y334F, pH 7, 25°C
41
benzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
48
benzyl alcohol
pH 6.0, 30°C
62
benzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
71
benzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
78
benzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
131
benzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
665
benzyl alcohol
mutant L416W, pH 7, 25°C
1020
benzyl alcohol
mutant L416F, pH 7, 25°C
5060
benzyl alcohol
wild-type, pH 7, 25°C
0.014
cinnamyl alcohol
pH 6, 30°C
3
cinnamyl alcohol
pH 7.5, 25°C
3.2
cinnamyl alcohol
pH 7.5, 25°C
2510
cinnamyl alcohol
-
pH 6.0, 30°C
0.0025
furan-2,5-dicarbaldehyde
-
pH 7, 25°C
0.003
furan-2,5-dicarbaldehyde
-
pH 7, 25°C
0.015
furan-2,5-dicarbaldehyde
pH 7, 25°C
13.3
isovanillyl alcohol
mutant L416W, pH 7, 25°C
27.3
isovanillyl alcohol
mutant L416F, pH 7, 25°C
167
isovanillyl alcohol
wild-type, pH 7, 25°C
1.9
Vanillyl alcohol
mutant L416W, pH 7, 25°C
21.8
Vanillyl alcohol
mutant L416F, pH 7, 25°C
2350
Vanillyl alcohol
wild-type, pH 7, 25°C
0.011
veratryl alcohol
pH 6, 30°C
0.97
veratryl alcohol
mutant Y334W, pH 7, 25°C
4.3
veratryl alcohol
mutant L416W, pH 7, 25°C
4.4
veratryl alcohol
mutant Y334F, pH 7, 25°C
4.7
veratryl alcohol
wild-type, pH 7, 25°C
8.3
veratryl alcohol
pH 7.5, 25°C
11
veratryl alcohol
pH 7.5, 25°C
28
veratryl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
29.3
veratryl alcohol
mutant L416F, pH 7, 25°C
36
veratryl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
72
veratryl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
102
veratryl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
132
veratryl alcohol
pH 6.0, 30°C
139
veratryl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
273
veratryl alcohol
wild-type, pH 7, 25°C
440
veratryl alcohol
-
pH 6.0, 30°C
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Y334F
mutant exhibits specific activities comparable to the wild-type for carbohydrates, diols, aryl alcohols, 5-hydroxymethylfurfural and 5-hydroxymethyl-2-furancarboxylic acid
Y334W
mutant exhibits increased specific activity toward carbohydrates and decreased activity toward diols, aryl alcohols, and furans
Y334F
-
mutant exhibits specific activities comparable to the wild-type for carbohydrates, diols, aryl alcohols, 5-hydroxymethylfurfural and 5-hydroxymethyl-2-furancarboxylic acid
-
Y334W
-
mutant exhibits increased specific activity toward carbohydrates and decreased activity toward diols, aryl alcohols, and furans
-
L416F
mutation decreases the activity with aromatic alcohols but maintains the activity with trans,trans-2,4-hexadien-1-ol
L416W
mutation decreases the activity with aromatic alcohols but maintains the activity with trans,trans-2,4-hexadien-1-ol
V367R/W466F
significant improvement of conversion rate
V465S
significant improvement of conversion rate
V465T
significant improvement of conversion rate and enantioselectivity with sec-allylic alcohols
V465T/W466H
significant improvement of conversion rate
A77W/R80C/H91N/L170M/V340A/I500M/F501W
best performer with substrate (S)-1-(4-methoxyphenyl)-ethanol, with a total 800fold enhancement of activity relative to the parental type
F397Y
mutant shows improved production of 2,5-furandicarboxylic acid, with 70% yield
F501H
mutant shows improved production of 2,5-furandicarboxylic acid, with 97% yield
F501W
site-directed mutagenesis, the mutant shows a twofold increase in O2 reactivity compared to the wild-type enzyme
H502L
-
site-directed mutagenesis, inactive mutant
H502R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H546A
site-directed mutagenesis, the mutant shows over 35fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme
H546L
-
site-directed mutagenesis, inactive mutant
H546R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H91N
-
random mutageneis, the FX7 mutant (harboring the H91N mutation) shows a dramatic 96fold improvement in total activity with secretion levels of 2 mg/liter. Analysis of the N-terminal sequence of the FX7 variant confirms the correct processing of the prealphaproK hybrid peptide by the KEX2 protease. FX7 shows higher stability in terms of pH and temperature, whereas the pH activity profiles and the kinetic parameters are maintained. The Asn91 lies in the flavin attachment loop motif, and it is a highly conserved residue in all members of the GMC superfamily, except for Pleurotus eryngii and Pleurotus pulmonarius AAO. FX7 mutant homology modeling using the crystal structure of the AAO from Pleurotus eryngii at a resolution of 2.55 A, PDB ID 3FIM, structure-function analysis
H91N/L170M/F501W
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/I500L/F501I
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500L/F501I present a 15fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol
H91N/L170M/I500M/F501V
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500M/F501V present a 30fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol
H91N/L170M/I500Q/F501W
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500Q/F501W present a 5fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol
I500M
mutant shows improved production of 2,5-furandicarboxylic acid, with 80% yield
I500M/F501 W
mutant shows improved production of 2,5-furandicarboxylic acid, reaching a total turnover number over 16,000 in presence of 15 mM 5-hydroxymethylfurfural
L315A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
synthesis
expression of AAO in the ascomycete Aspergillus nidulans. The activity of the recombinant enzyme in Aspergillus nidulans cultures is much higher than found in the extracellular fluid of Pleurotus eryngii. The recombinant enzyme shows the same molecular mass, pI and catalytic properties as that of the mature protein secreted by Pleurotus eryngii
Y78A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
Y92A
-
site-directed mutagenesis, inactive mutant
F501A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F501A
-
site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview
F501A
site-directed mutagenesis, the mutant shows strongly reduced O2 reactivity compared to the wild-type enzyme
F501A
the AAO preference for (S)-1-(4-fluorophenyl)ethanol is increased threefold when the bulky side chain of Phe501 is removed in the F501A variant, which shows a stereoselectivity S/R ratio of 66:1 for this secondary alcohol
F501Y
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F501Y
-
site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview
H502A
site-directed mutagenesis, the mutant shows 3000fold and 1800fold decreased kcat and kred compared to the wild-type enzyme
H502A
site-directed mutagenesis, the mutant shows over 1800fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity, compared to the wild-type enzyme
H502S
-
site-directed mutagenesis, inactive mutant
H502S
the mutant shows much lower activities on 4-nitrobenzaldehyde (340fold activity decrease) than the wild type enzyme
H502S
site-directed mutagenesis, the mutant shows over 1200fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme
H546S
-
site-directed mutagenesis, inactive mutant
H546S
the mutant shows much lower activities on 4-nitrobenzaldehyde (670fold activity decrease) than the wild type enzyme
H546S
site-directed mutagenesis, the mutant shows decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme
H91N/L170M
expression variant carrying 4 mutations in the chimeric signal peptide (prealphaproK), plus mutations H91N/L170M in the mature protein, shows increased secretion upon expression in Pichia pastoris and Saccharomyces cerevisiae
H91N/L170M
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/I500M/F501W
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/I500M/F501W
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500M/F501W present a 160fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol, while the specific activity on primary alcohols is dramatically reduced
Y92F
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
Y92F
the mutation causes a 5fold reduction in the p-anisaldehyde kcat value
Y92F
site-directed mutagenesis, replacement of Tyr92 by phenylalanine does not alter the AAO kinetic constants (on 4-methoxybenzyl alcohol), compared to the wild-type enzyme, most probably because the stacking interaction is still possible
Y92F
mutation of active site, residue is involved in modulating the hydride transfer reaction
Y92L
site-directed mutagenesis, replacement with a leucine produces a decrease in catalytic efficiency for the alcohol substrate (2.6fold lower), accompanied by approximately twofold increases in both Km(Al) and Kd compared to the wild-type enzyme. The mutation causes a strong decrease in catalytic efficiencies for both O2 (6fold lower) and 4-methoxybenzyl alcohol (860fold lower). As the turnover rate for the Y92W variant is reduced tenfold, the main effect of the mutation concerns the availability of the alcohol substrate at the AAO active site (with 75fold higher Km values). The stacking interactions are strongly affected by this mutation
Y92L
mutation of active site, residue is involved in modulating the hydride transfer reaction
Y92W
site-directed mutagenesis, introduction of a tryptophan residue at this position only causes a slight increase in KMO2, but strongly reduces the affinity for the substrate (i.e. the pre-steady state Kd and steady-state Km increase by 150fold and 75fold, respectively) and therefore the steady-state catalytic efficiency, compared to the wild-type enzyme, suggesting that proper stacking is impossible with this bulky residue
Y92W
mutation of active site, residue is involved in modulating the hydride transfer reaction
additional information
-
wild-type and mutant enzymes are adsorbed on graphite electrodes or with the enzymes in solution using glassy carbon electrode as working electrode, activity analysis, overview
additional information
-
in vitro involution of the enzyme by restoring the consensus ancestor Asn91 promotes AAO expression and stability. The native signal sequence of AAO from Pleurotus eryngii is replaced by those of the mating alpha-factor and the K1 killer toxin, as well as different chimeras of both prepro-leaders in order to drive secretion in Saccharomyces cerevisiae strain BJ5465. The secretion of these mutant AAO constructs increase in the following descending order: preproalpha-AAO, prealphaproK-AAO, preKproalpha-AAO, preproK-AAO. The chimeric prealphaproK-AAO is subjected to focused-directed evolution with the aid of a dual screening assay based on the Fenton reaction. Random mutagenesis and DNA recombination is concentrated on two protein segments (Met[alpha1]-Val109 and Phe392-Gln566), and an array of improved variants is identified
additional information
a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5
additional information
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5
additional information
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5
-
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Muheim, A.; Leisola, M.S.A.; Schoemaker, H.E.
Aryl-alcohol oxidase and lignin peroxidase from the white-rot fungus Bjerkandera adusta
J. Biotechnol.
13
159-167
1990
Bjerkandera adusta, no activity in Phanerochaete chrysosporium
-
brenda
Guillen, F.; Martinez, A.T.; Martinez, M.J.
Production of hydrogen peroxide by aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryhgii
Appl. Microbiol. Biotechnol.
32
465-469
1990
Pleurotus eryngii
-
brenda
Muheim, A.; Waldner, R.; Leisola, M.S.A.; Fiechter, A.
An extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta
Enzyme Microb. Technol.
12
204-209
1990
Bjerkandera adusta
-
brenda
Waldner, R.; Leisola, M.S.A.; Fiechter, A.
Comparison of ligninolytic activities of selected white-rot fungi
Appl. Microbiol. Biotechnol.
29
400-407
1988
Bjerkandera adusta, Phanerodontia chrysosporium, Trametes versicolor, Rigidoporus microporus, Pleurotus ostreatus
-
brenda
Bourbonnais, R.; Paice, M.G.
Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju
Biochem. J.
255
445-450
1988
Lentinus sajor-caju
brenda
Farmer, V.C.; Henderson, M.E.K.; Russell, J.D.
Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor
Biochem. J.
74
257-262
1960
Trametes versicolor
brenda
Mann, V.; Large, A.; Khan, S.; Malik, Z.; Connock, M.J.
Aromatic alcohol oxidase: a new membrane-bound H2O2-generating enzyme in alimentary tiddues of the slug Arion ater
J. Exp. Zool.
251
265-274
1989
Arion ater
-
brenda
Marzullo, L.; Cannio, R.; Giardina, P.; Santini, M.T.; Sannia, G.
Veratryl alcohol oxidase from Pleurotus ostreatus participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates
J. Biol. Chem.
270
3823-3827
1995
Pleurotus ostreatus
brenda
Varela, E.; Martinez, A.T.; Martinez, M.J.
Molecular cloning of aryl-alcohol oxidase from the fungus Pleurotus eryngii, an enzyme involved in lignin degradation
Biochem. J.
341
113-117
1999
Pleurotus eryngii
-
brenda
Varela, E.; Guillen, F.; Martinez, A.T.; Martinez, M.J.
Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans: purification and characterization of the recombinant enzyme
Biochim. Biophys. Acta
1546
107-113
2001
Pleurotus eryngii
brenda
Varela, E.; Bockle, B.; Romero, A.; Martinez, A.T.; Martinez, M.J.
Biochemical characterization, cDNA cloning and protein crystallization of aryl-alcohol oxidase from Pleurotus pulmonarius
Biochim. Biophys. Acta
1476
129-138
2000
Pleurotus pulmonarius
brenda
Asada, Y.; Watanabe, A.; Ohtsu, Y.; Kuwahara, M.
Purification and characterization of an aryl-alcohol oxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium
Biosci. Biotechnol. Biochem.
59
1339-1341
1995
Phanerodontia chrysosporium
-
brenda
Guillen, F.; Martinez, A.T.; Martinez, M.J.
Substrate specificity and properties of the aryl-alcohol oxidase from ligninolytic fungus Pleurotus eryngii
Eur. J. Biochem.
209
603-611
1992
Pleurotus eryngii
brenda
Brckmann, M.; Termonia, A.; Pasteels, J.M.; Hartmann, T.
Characterization of an extracellular salicyl alcohol oxidase from larval defensive secretions of Chrysomela populi and Phratora vitellinae (Chrysomelina)
Insect Biochem. Mol. Biol.
32
1517-1523
2002
Chrysomela populi, Phratora vitellinae
brenda
Okamoto, K.; Yanase, H.
Aryl alcohol oxidases from the white-rot basidiomycete Pleurotus ostreatus
Mycoscience
43
391-395
2002
Pleurotus ostreatus
-
brenda
Kumar, A.K.; Goswami, P.
Functional characterization of alcohol oxidases from Aspergillus terreus MTCC 6324
Appl. Microbiol. Biotechnol.
72
906-911
2006
Aspergillus terreus, Aspergillus terreus MTCC 6324
brenda
Ferreira, P.; Medina, M.; Guillen, F.; Martinez, M.J.; Van Berkel, W.J.; Martinez, A.T.
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated alcohols
Biochem. J.
389
731-738
2005
Pleurotus eryngii
brenda
Sampedro, I.; DAnnibale, A.; Ocampo, J.A.; Stazi, S.R.; Garcia-Romera, I.
Solid-state cultures of Fusarium oxysporum transform aromatic components of olive-mill dry residue and reduce its phytotoxicity
Biores. Technol.
98
3547-3554
2007
no activity in Fusarium oxysporum, no activity in Fusarium oxysporum BAFC 738
brenda
D'Annibale, A.; Ricci, M.; Leonardi, V.; Quaratino, D.; Mincione, E.; Petruccioli, M.
Degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil
Biotechnol. Bioeng.
90
723-731
2005
no activity in Phanerochaete chrysosporium, Pleurotus pulmonarius, no activity in Phanerochaete chrysosporium NRRL 6361
brenda
Kabe, Y.; Osawa, T.; Ishihara, A.; Kabe, T.
Decolorization of coal humic acid by extracellular enzymes produced by white-rot fungi
Coal Prep.
25
211-220
2005
Pleurotus pulmonarius
-
brenda
Ferreira, P.; Ruiz-Duenas, F.J.; Martinez, M.J.; van Berkel, W.J.; Martinez, A.T.
Site-directed mutagenesis of selected residues at the active site of aryl-alcohol oxidase, an H2O2-producing ligninolytic enzyme
FEBS J.
273
4878-4888
2006
Pleurotus eryngii
brenda
Saparrata, M.C.; Guillen, F.
Ligninolytic ability and potential biotechnology applications of the south american fungus Pleurotus laciniatocrenatus
Folia Microbiol. (Praha)
50
155-160
2005
Pleurotus laciniatocrenatus
brenda
Madhurendr, M.; Prasad, N.
Veratryl alcohol oxidase and laccase activity in Pleurotus spp
J. Plant Biol.
32
129-132
2005
Pleurotus ostreatus, Lentinus sajor-caju
-
brenda
Ruiz-Duenas, F.J.; Ferreira, P.; Martinez, M.J.; Martinez, A.T.
In vitro activation, purification, and characterization of Escherichia coli expressed aryl-alcohol oxidase, a unique H2O2-producing enzyme
Protein Expr. Purif.
45
191-199
2006
Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Michalski, C.; Mohagheghi, H.; Nimtz, M.; Pasteels, J.; Ober, D.
Salicyl alcohol oxidase of the chemical defense secretion of two chrysomelid leaf beetles: Molecular and functional characterization of two new members of the GMC oxidoreductase gene family
J. Biol. Chem.
283
19219-19228
2008
Chrysomela tremula (B4F334), Chrysomela tremula, Chrysomela populi (B4F335), Chrysomela populi
brenda
Ferreira, P.; Hernandez-Ortega, A.; Herguedas, B.; Martinez, A.T.; Medina, M.
Aryl-alcohol oxidase involved in lignin degradation: a mechanistic study based on steady and pre-steady state kinetics and primary and solvent isotope effects with two alcohol substrates
J. Biol. Chem.
284
24840-24847
2009
Pleurotus eryngii (O94219)
brenda
Munteanu, F.; Ferreira, P.; Ruiz-Duenas, F.; Martinez, A.; Cavaco-Paulo, A.
ioelectrochemical investigations of aryl-alcohol oxidase from Pleurotus eryngii
J. Electroanal. Chem.
618
83-86
2008
Pleurotus eryngii
-
brenda
Fernandez, I.S.; Ruiz-Duenas, F.J.; Santillana, E.; Ferreira, P.; Martinez, M.J.; Martinez, A.T.; Romero, A.
Novel structural features in the GMC family of oxidoreductases revealed by the crystal structure of fungal aryl-alcohol oxidase
Acta Crystallogr. Sect. D
65
1196-1205
2009
Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Kumar, V.V.; Rapheal, V.S.
Induction and purification by three-phase partitioning of aryl alcohol oxidase (AAO) from Pleurotus ostreatus
Appl. Biochem. Biotechnol.
163
423-432
2011
Pleurotus ostreatus
brenda
Ferreira, P.; Hernandez-Ortega, A.; Herguedas, B.; Rencoret, J.; Gutierrez, A.; Martinez, M.J.; Jimenez-Barbero, J.; Medina, M.; Martinez, A.T.
Kinetic and chemical characterization of aldehyde oxidation by fungal aryl-alcohol oxidase
Biochem. J.
425
585-593
2010
Pleurotus eryngii (O94219)
brenda
Lupo, S.; Perez, A.; Martinez, S.; Simeto, S.; Rivas, F.; Bettucci, L.
In vitro characterization of Inocutis jamaicensis and experimental inoculation of Eucalyptus globulus standing trees
Forest Pathol.
39
293-303
2009
no activity in Inocutis jamaicensis
brenda
Hernandez-Ortega, A.; Ferreira, P.; Martinez, A.T.
Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation
Appl. Microbiol. Biotechnol.
93
1395-1410
2012
Bjerkandera adusta, Botrytis cinerea, Phanerodontia chrysosporium, Trametes versicolor, Rigidoporus microporus, Fusarium solani, Postia placenta, Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Hernandez-Ortega, A.; Borrelli, K.; Ferreira, P.; Medina, M.; Martinez, A.T.; Guallar, V.
Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase
Biochem. J.
436
341-350
2011
Pleurotus eryngii (O94219)
brenda
Hernandez-Ortega, A.; Lucas, F.; Ferreira, P.; Medina, M.; Guallar, V.; Martinez, A.T.
Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle
Biochemistry
51
6595-6608
2012
Pleurotus eryngii (O94219)
brenda
Tamboli, D.; Telke, A.; Dawkar, V.; Jadhav, S.; Govindwar, S.
Purification and characterization of bacterial aryl alcohol oxidase from Sphingobacterium sp. ATM and its uses in textile dye decolorization
Biotechnol. Bioprocess Eng.
16
661-668
2011
Sphingobacterium sp., Sphingobacterium sp. ATM
-
brenda
Hernandez-Ortega, A.; Ferreira, P.; Merino, P.; Medina, M.; Guallar, V.; Martinez, A.T.
Stereoselective hydride transfer by aryl-alcohol oxidase, a member of the GMC superfamily
ChemBioChem
13
427-435
2012
Pleurotus eryngii (O94219)
brenda
Hernandez-Ortega, A.; Lucas, F.; Ferreira, P.; Medina, M.; Guallar, V.; Martinez, A.T.
Modulating O2 reactivity in a fungal flavoenzyme: involvement of aryl-alcohol oxidase Phe-501 contiguous to catalytic histidine
J. Biol. Chem.
286
41105-41114
2011
Pleurotus eryngii (O94219)
brenda
Chakraborty, M.; Goel, M.; Chinnadayyala, S.R.; Dahiya, U.R.; Ghosh, S.S.; Goswami, P.
Molecular characterization and expression of a novel alcohol oxidase from Aspergillus terreus MTCC6324
PLoS ONE
9
e95368
2014
Aspergillus terreus (I7FDJ2), Aspergillus terreus MTCC6324 (I7FDJ2)
brenda
Vina-Gonzalez, J.; Gonzalez-Perez, D.; Ferreira, P.; Martinez, A.T.; Alcalde, M.
Focused directed evolution of aryl-alcohol oxidase in Saccharomyces cerevisiae by using chimeric signal peptides
Appl. Environ. Microbiol.
81
6451-6462
2015
Pleurotus eryngii
brenda
Couturier, M.; Mathieu, Y.; Li, A.; Navarro, D.; Drula, E.; Haon, M.; Grisel, S.; Ludwig, R.; Berrin, J.G.
Characterization of a new aryl-alcohol oxidase secreted by the phytopathogenic fungus Ustilago maydis
Appl. Microbiol. Biotechnol.
100
697-706
2016
Ustilago maydis
brenda
Galperin, I.; Javeed, A.; Luig, H.; Lochnit, G.; Ruehl, M.
An aryl-alcohol oxidase of Pleurotus sapidus heterologous expression, characterization, and application in a 2-enzyme system
Appl. Microbiol. Biotechnol.
100
8021-8030
2016
Pleurotus sapidus (A0A145Y386), Pleurotus sapidus, Pleurotus sapidus DSM 8266 (A0A145Y386)
brenda
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