1.1.3.7: aryl-alcohol oxidase
This is an abbreviated version!
For detailed information about aryl-alcohol oxidase, go to the full flat file.
Word Map on EC 1.1.3.7
-
1.1.3.7
-
anodic
-
aluminum
-
fabric
-
nanoporous
-
porous
-
film
-
nanostructures
-
ascending
-
aorta
-
lignin
-
nanowires
-
nanotube
-
laccase
-
etch
-
nanochannels
-
ophthalmology
-
age-at-onset
-
academy
-
decolor
-
nanorods
-
pleurotus
-
ligninolytic
-
white-rot
-
bicuspid
-
free-standing
-
eryngii
-
electrodeposition
-
sputter
-
valsalva
-
large-area
-
template-assisted
-
environmental protection
-
synthesis
-
aortopathy
-
bjerkandera
-
nanopillars
-
four-dimensional
-
nanopatterns
-
photovoltaic
-
polycrystalline
-
remazol
-
glucose-methanol-choline
-
president
-
nanoarrays
- 1.1.3.7
-
anodic
-
aluminum
-
fabric
-
nanoporous
-
porous
-
film
-
nanostructures
-
ascending
-
aorta
- lignin
-
nanowires
-
nanotube
- laccase
-
etch
-
nanochannels
-
ophthalmology
-
age-at-onset
-
academy
-
decolor
-
nanorods
- pleurotus
-
ligninolytic
-
white-rot
-
bicuspid
-
free-standing
- eryngii
-
electrodeposition
-
sputter
-
valsalva
-
large-area
-
template-assisted
- environmental protection
- synthesis
-
aortopathy
- bjerkandera
-
nanopillars
-
four-dimensional
-
nanopatterns
-
photovoltaic
-
polycrystalline
-
remazol
-
glucose-methanol-choline
-
president
-
nanoarrays
Reaction
Synonyms
AAO, AAO2, AAOx, alcohol: O2 oxidoreductase, AOX, arom. alcohol oxidase, aryl alcohol oxidase, arylalcohol oxidase, CpSAO, CtSAO, GaoB, GLRG_02805, GMC oxidoreductase-like protein, HMFO, More, MtGloA, MYCTH_2299749, oxidase, aryl alcohol, salicyl alcohol oxidase, um04044, VAO, veratryl alcohol oxidase
ECTree
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Substrates Products
Substrates Products on EC 1.1.3.7 - aryl-alcohol oxidase
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REACTION DIAGRAM
(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,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
-
-
?
(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-naphthalene methanol + O2
alpha-naphthaldehyde + H2O2
-
27% of the activity with cinnamyl alcohol
-
-
?
2-anisyl alcohol + O2
2-anisyl aldehyde + H2O2
96% of the activity with benzyl alcohol
-
-
?
2-methoxybenzyl alcohol + O2
2-methoxybenzaldehyde + H2O
-
23% of the activity with 2-hydroxybenzyl alcohol
-
?
2-naphthalenemethanol + O2
2-naphthaleneformaldehyde + H2O
-
745.7% of the activity with benzyl alcohol
-
?
3,4-difluorobenzaldehyde + O2
3,4-difluorobenzoic acid + H2O2
-
-
-
?, r
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-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-fluorobenzyl alcohol + O2
3-fluorobenzyl aldehyde + H2O2
-
low activity
-
-
?
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-hydroxybenzyl aldehyde + H2O2
221% of the activity with benzyl alcohol
-
-
?
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-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + 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
-
-
?
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
-
?
veratryl alcohol + 2,6-dichlorophenol indophenol
veratrylaldehyde + red. 2,6-dichlorophenol indophenol
-
-
-
-
?
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
63.9% of the activity with benzyl alcohol
-
-
?
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
-
-
?
1-(4-fluorophenyl)acetaldehyde + H2O2
-
-
-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
mutant F501A
-
-
?
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-dimethoxybenzaldehyde + H2O2
-
-
-
r
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
177.5% of the activity with benzyl alcohol
-
?
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
-
-
?
? + H2O2
-
531% of the activity with benzyl alcohol
-
?
5-formylfuran-2-carboxylic acid + ?
-
-
-
?
2,5-diformylfuran + O2
5-formylfuran-2-carboxylic acid + ?
-
-
-
?
formylfurancarboxylic acid + ?
-
-
-
?
2,6-dichloroaniline + O2
?
-
degradation, complete removal from soil
-
-
?
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
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-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-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
best substrate
-
-
r
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-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
-
-
?
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 aldehyde + H2O2
297% of the activity with benzyl alcohol
-
-
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
ping-pong mechanism
-
-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
ping-pong mechanism
-
-
?
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-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
-
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
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl aldehyde + H2O2
298% of the activity with benzyl alcohol
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
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-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 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-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
-
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
-
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl aldehyde + H2O2
-
-
-
?
furan-2,5-dicarboxylic acid + ?
-
-
-
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
furan-2,5-dicarboxylic acid + ?
-
-
-
?
furan-2,5-dicarbaldehyde + H2O2
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
-
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
-
-
-
?
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
-
-
-
-
?
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
Thermothelomyces thermophilus DSM 1799
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
2,5-furandicarboxylic acid + ?
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-furandicarboxylic acid + ?
-
-
-
-
?
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
-
-
?
7H-benz[DE]anthracen-7-one + O2
?
-
degradation, partial removal from soil
-
-
?
9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
anisyl alcohol + O2
anisaldehyde + H2O2
best substrate
-
-
?
anisyl aldehyde + H2O2
647% of the activity with benzyl alcohol
-
-
?
benzaldehyde + H2O2
-
26% of the activity with cinnamyl alcohol
-
-
?
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
-
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
-
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
-
3.6% of the activity with 4-methoxybenzyl alcohol
-
-
?
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
-
451.1% of the activity with benzyl alcohol
-
?
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 aldehyde + H2O2
289% of the activity with benzyl alcohol
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
442% of the activity with benzyl alcohol
-
-
?
2,5-furandicarboxylic acid + H2O2
-
-
-
?
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
-
?
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 aldehyde + H2O2
73% of the activity with benzyl alcohol
-
-
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
246% of the activity with benzyl alcohol
-
-
?
N-phenyl-1-naphthalenamine + O2
?
-
degradation, complete removal from soil
-
-
?
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
322% of the activity with benzyl alcohol
-
-
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
i.e. 3,4-dimethoxybenzyl alcohol
-
-
?
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
Thermothelomyces thermophilus DSM 1799
no substrates: glucose, cellobiose, methanol
-
-
-
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
-
-
?