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(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
mutant F501A
-
-
?
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
-
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-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 + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
ir
2,6-dichloroaniline + O2
?
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
-
-
-
?
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-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-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
3-methoxybenzyl alcohol + O2
3-methoxybenzylaldehyde + H2O
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-anisaldehyde + O2
4-anisic acid + H2O2
-
-
-
r
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
-
7.6% of the activity with anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
-
-
-
r
4-nitrobenzaldehyde + O2
4-nitrobenzoic acid
-
-
-
?
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-furandicarboxylic acid + H2O2
very low activity
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
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
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
-
-
?
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
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
-
-
-
-
?
m-anisyl alcohol + O2
m-anisaldehyde + H2O2
N-phenyl-1-naphthalenamine + O2
?
n-propanol + O2
propionaldehyde + 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
?
-
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-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
-
-
-
-
?
2,6-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
-
-
-
-
?
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
-
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-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
-
-
-
-
?
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-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
-
-
-
r
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
-
-
-
?
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
-
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
-
-
-
-
?
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
-
-
?
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
-
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
-
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
-
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
-
-
-
-
?
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
-
-
-
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
-
-
?
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
-
-
?
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

veratryl aldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
-
-
?
1,1'-binaphthalene + O2
?
-
degradation, partial removal from soil
-
-
?
1,2,3,4,5-pentachlorobenzene + O2
?
-
degradation, partial removal from soil
-
-
?
1,2,3,4-tetrachlorobenzene + O2
?
-
degradation, complete removal from soil
-
-
?
1,2,4,5-tetrachlorobenzene + O2
?
-
degradation, complete removal from soil
-
-
?
1,2-binaphthalene + O2
?
-
degradation, partial removal from soil
-
-
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
degradation, partial removal from soil
-
-
?
1-amino-9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
1-chloro-9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
2,4-dichloroaniline + O2
?
-
degradation, complete removal from soil
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
-
-
r
2,4-hexadien-1-ol + O2
?
-
-
-
?
2,5-diformylfuran + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
ir
2,6-dichloroaniline + O2
?
-
degradation, complete removal from soil
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
-
-
r
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
r
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
-
-
-
r
4-nitrobenzyl alcohol + O2
4-nitrobenzaldehyde + H2O2
-
-
-
r
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
7H-benz[DE]anthracen-7-one + O2
?
-
degradation, partial removal from soil
-
-
?
9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
high activity
-
-
r
diphenylether + O2
?
-
degradation, complete removal from soil
-
-
?
diphenylsulfone + O2
?
-
degradation, partial removal from soil
-
-
?
N-phenyl-1-naphthalenamine + O2
?
-
degradation, complete removal from soil
-
-
?
n-propanol + O2
propionaldehyde + H2O2
naphthalene + O2
?
-
degradation, complete removal from soil
-
-
?
veratryl alcohol + O2
veratraldehyde + H2O2
veratryl alcohol + O2
veratryl aldehyde + H2O2
Pleurotus laciniatocrenatus
-
-
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
-
-
-
?
additional information
?
-
2-hydroxybenzyl alcohol + O2

2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
-
-
?
4-methoxybenzyl alcohol + O2

4-methoxybenzaldehyde + H2O2
-
-
-
?
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
-
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl 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
-
-
-
-
?
n-propanol + O2

propionaldehyde + H2O2
-
-
-
-
?
n-propanol + O2
propionaldehyde + H2O2
-
-
-
-
?
veratryl alcohol + O2

veratraldehyde + H2O2
-
-
-
r
veratryl alcohol + O2
veratraldehyde + H2O2
-
-
-
-
?
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 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
?
-
-
production of H2O2 during oxidation of lignin fragments
-
-
?
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
?
-
-
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
?
-
-
AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
-
-
?
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
?
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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
2,5-diformylfuran
pH 6.0, 25°C
-
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
0.211 - 0.734
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
0.22 - 4.91
3-Methoxybenzyl alcohol
0.015 - 0.053
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
4-Hydroxybenzyl alcohol
-
pH 6.0, 30°C
0.017 - 3.82
4-methoxybenzyl alcohol
2 - 5
4-nitrobenzaldehyde
1.6
5-hydroxymethylfurfural
pH 6.0, 25°C
0.0048 - 0.836
anisyl alcohol
7
benzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.03 - 10.8
benzyl alcohol
0.035 - 0.708
cinnamyl alcohol
0.831
isovanillyl alcohol
-
pH 6.0, 24°C
0.22 - 0.3
m-anisyl alcohol
0.03
p-anisyl alcohol
-
recombinant enzyme
0.025
Vanillyl alcohol
-
-
8
veratraldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.027 - 2
veratryl alcohol
additional information
additional information
-
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
0.113
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
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
0.211
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
0.227
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
0.301
3-anisyl alcohol
-
pH 6.0, 24°C, mutant Y92F
0.734
3-anisyl alcohol
-
pH 6.0, 24°C, mutant F501A
0.22
3-Methoxybenzyl alcohol

-
pH 6.0, 25°C
4.91
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°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
0.015
4-anisyl alcohol

-
pH 6.0, 24°C, mutant F501Y
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
-
-
0.037
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
0.053
4-anisyl alcohol
-
pH 6.0, 24°C, mutant Y78A
0.017
4-methoxybenzyl alcohol

pH 6.0, 25°C, mutant F501Y, overall reaction
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
0.029
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
0.034
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
0.04
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
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
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
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
0.388
benzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
0.39
benzyl alcohol
-
wild-type enzyme expressed in Escherichia coli
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
0.632
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
0.873
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
0.035
cinnamyl alcohol

-
pH 6.0, 30°C
0.708
cinnamyl 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
0.027
veratryl alcohol

-
wild-type enzyme expressed in Emericella nidulans
0.044
veratryl alcohol
-
mutant F501A expressed in Emericella nidulans
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
0.38
veratryl alcohol
-
pH 6.0, 24°C, mutant F501A
0.41
veratryl alcohol
pH 8.0, 25°C, wild-type enzyme
0.46
veratryl alcohol
-
pH 6.0, 24°C, mutant Y92F
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
0.59 - 1
veratryl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.6
veratryl alcohol
-
pH 6.0, 40°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
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
-
MichaelisâMenten 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
-
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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
31.4
2,5-diformylfuran
pH 6.0, 25°C
-
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
115.4
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.012 - 0.05
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
75
4-Hydroxybenzyl alcohol
-
pH 6.0, 30°C
0.069 - 208
4-methoxybenzyl alcohol
1.21 - 1.633
4-nitrobenzaldehyde
20.1
5-hydroxymethylfurfural
pH 6.0, 25°C
0.5
benzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
127
isovanillyl alcohol
-
pH 6.0, 24°C
8.27
m-anisyl alcohol
-
-
48.5
p-anisyl alcohol
-
-
0.13
veratraldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
1
2,4-hexadien-1-ol

-
pH 6.0, 24°C, mutant F501A
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
64
2,4-hexadien-1-ol
-
pH 6.0, 30°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
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
8
3-anisyl alcohol
-
pH 6.0, 24°C, mutant Y78A
12
3-anisyl alcohol
-
pH 6.0, 24°C, mutant L315A
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
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
3
4-anisyl alcohol

-
pH 6.0, 24°C, mutant F501A
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
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
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
40
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
54
4-methoxybenzyl alcohol
-
recombinant H91N FX7 mutant, pH 6.0, 24°C
64
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
87
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, overall reaction
100
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92L
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
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
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
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
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
33
benzyl alcohol
-
pH 6.0, 24°C, mutant Y92F
38
benzyl alcohol
pH 6.0, 30°C
65
cinnamyl alcohol

-
pH 6.0, 24°C
88
cinnamyl alcohol
-
pH 6.0, 30°C
2 - 8
veratryl alcohol

-
recombinant H91N FX7 mutant, pH 6.0, 24°C
3
veratryl alcohol
-
pH 6.0, 24°C, mutant F501A
53
veratryl alcohol
-
pH 6.0, 30°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
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