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
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1.1.3.7
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anodic
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aluminum
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fabric
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nanoporous
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porous
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film
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nanostructures
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ascending
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aorta
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lignin
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nanowires
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nanotube
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laccase
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etch
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nanochannels
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ophthalmology
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age-at-onset
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academy
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decolor
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nanorods
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pleurotus
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ligninolytic
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white-rot
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bicuspid
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free-standing
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eryngii
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electrodeposition
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sputter
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valsalva
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large-area
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template-assisted
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environmental protection
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synthesis
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aortopathy
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bjerkandera
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nanopillars
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four-dimensional
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nanopatterns
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photovoltaic
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polycrystalline
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remazol
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glucose-methanol-choline
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president
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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
1.1.3.7 aryl-alcohol oxidaseAdvanced search results
results (
results (Natural Substrates Products
Natural Substrates Products on EC 1.1.3.7 - aryl-alcohol oxidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
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-
?
1,1'-binaphthalene + O2
?
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degradation, partial removal from soil
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-
?
1,2,3,4,5-pentachlorobenzene + O2
?
-
degradation, partial removal from soil
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-
?
1,2,3,4-tetrachlorobenzene + O2
?
-
degradation, complete removal from soil
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-
?
1,2,4,5-tetrachlorobenzene + O2
?
-
degradation, complete removal from soil
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-
?
1,2-binaphthalene + O2
?
-
degradation, partial removal from soil
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-
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
degradation, partial removal from soil
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-
?
1-amino-9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
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-
?
1-chloro-9,10-anthracenedione + O2
?
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degradation, partial removal from soil
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-
?
2,4-dichloroaniline + O2
?
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degradation, complete removal from soil
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-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
-
-
r
2,6-dichloroaniline + O2
?
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degradation, complete removal from soil
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-
?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
-
-
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
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-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
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?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
r
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
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-
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r
7H-benz[DE]anthracen-7-one + O2
?
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degradation, partial removal from soil
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-
?
9,10-anthracenedione + O2
?
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degradation, partial removal from soil
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-
?
N-phenyl-1-naphthalenamine + O2
?
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degradation, complete removal from soil
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-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
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?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
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?
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
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r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol
-
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?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
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?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
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-
?
additional information
?
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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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-
?
additional information
?
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-
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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?
additional information
?
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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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?
additional information
?
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production of H2O2 during oxidation of lignin fragments
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?
additional information
?
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the enzyme is involved in lignin degradation
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?
additional information
?
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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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-
?
additional information
?
-
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the enzyme is involved in lignin degradation
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-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
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-
?
additional information
?
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the enzyme provides H2O2 for fungal degradation of lignin
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?
additional information
?
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the enzyme provides H2O2 for fungal degradation of lignin
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?
additional information
?
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AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
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-
?
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
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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
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?
additional information
?
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the enzyme participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates
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?
additional information
?
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the enzyme is involved in lignin degradation
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?
additional information
?
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decolorization of coal humic acid by the extracellular enzyme produced by white-rot fungi, low activity, overview
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?
additional information
?
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degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil, e.g. from chemical industrial sites, overview
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?
additional information
?
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-
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
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-
?
