HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.1.3.7 - aryl-alcohol oxidase
for references in articles please use BRENDA:EC1.1.3.7
Word Map on EC 1.1.3.7
- 1.1.3.7
-
anodic
-
aluminum
-
fabric
-
pore
-
nanoporous
-
porous
-
nanostructures
-
film
-
nanowires
-
lignin
-
nanotube
- laccase
-
ascending
-
nanorods
- pleurotus
-
etch
-
academy
-
electrodeposition
-
nanochannels
- eryngii
-
ligninolytic
-
decolor
-
ophthalmology
-
age-at-onset
-
cylindrical
-
bicuspid
-
white-rot
-
president
-
free-standing
-
sputter
-
glucose-methanol-choline
-
orthodontic
-
photovoltaic
-
textile
-
surface-enhanced
-
photoluminescence
- dcip
-
polycrystalline
- environmental protection
-
remazol
- biofuel production
-
nanopatterns
- bjerkandera
- synthesis
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.1.3.7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
aryl-alcohol oxidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
-
-
-
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, the enzyme does not thermodynamically stabilize a flavin semiquinone radical and forms no sulphite adduct
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, active site structure, Tyr92, Phe501, His502 and His546 are strictly required for activity, Tyr78 is not involved in catalysis, while Leu315 might be important
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
a sequential mechanism in which O2 reacts with reduced enzyme before release of the aldehyde product, the AAO reductive half-reaction is essentially irreversible and rate limiting during catalysis, a synchronous mechanism in which hydride transfer from substrate alpha-carbon to FAD and proton abstraction from hydroxyl occur simultaneously, reaction mechanism, overview. The AAO catalytic mechanism proceeds via electrophilic attack and direct transfer of a hydride to the flavin
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
catalytic mechanism with catalytic cycle including two half-reactions, overview. Proton transfer to His502 acting as a base, His546 plays a role in alcohol binding. Phe501 forces O2 to approach the flavin C4a, and His502 yielding hydrogen peroxide and the reoxidized flavin
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
modeling protein-ligand recognition mechanisms, substrate diffusion into the AAO active site, two conserved histidine residues, His502 and His546, are involved in catalysis, structure-function analysis, overview
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
two conserved histidine residues, His502 and His546, are involved in catalysis and play roles in the two half-reactions, with a stronger histidine involvement in the reductive than in the oxidative half-reaction. His502 is the catalytic base in the AAO reductive half-reaction. The His502 proton transfer does not limit the oxidative half-reaction, stereoselective hydride transfer. Quantum mechanical/molecular mechanical study, mutational analysis, and computational simulations, detailed overview
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
oxidation mechanism by AAO, overview
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
kinetic and reaction mechanisms involving residue Tyr92, hydride transfer reaction and aromatic stacking interactions on catalysis. Sequential reaction mechanism involving a ternary complex between AAO and its reducing/oxidizing substrates versus a ping-pong mechanism, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
aryl-alcohol:oxygen oxidoreductase
Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-77-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis by mixed quantum mechanics/molecular mechanics studies, overview
evolution
-
the enzyme belongs to the glucose–methanol–choline oxidase superfamily
evolution
-
the enzyme belongs to the glucose methanol choline oxidase superfamily
evolution
the enzyme is a member of the glucosemethanol-choline oxidase (GMC) oxidoreductase superfamily and the AAO family. Phylogenetic analysis of the AAOs in Pleurotus ostreatous revealed that they cluster into two groups
evolution
-
the enzyme is a member of the glucosemethanol-choline oxidase (GMC) oxidoreductase superfamily and the AAO family. Phylogenetic analysis of the AAOs in Pleurotus ostreatous revealed that they cluster into two groups
-
metabolism
-
aryl-alcohol oxidase, AAO, participates in fungal degradation of lignin, a process of high ecological and biotechnological relevance, by providing the hydrogen peroxide required by ligninolytic peroxidases, mechanism, overview
metabolism
-
the enzyme is important in the 5-hydroxymethylfurfural degradation pathway, verview
physiological function
-
aryl-alcohol oxidase, AAO, participates in fungal degradation of lignin, a process of high ecological and biotechnological relevance, by providing the hydrogen peroxide required by ligninolytic peroxidases, mechanism, overview
physiological function
-
aryl-alcohol oxidase provides hydrogen peroxide necessary for peroxidase activity during lignin biodegradation
physiological function
-
aryl alcohol oxidase is involved in lignin degradation
physiological function
-
aryl-alcohol oxidase provides H2O2 for lignin biodegradation
physiological function
-
the enzyme is part of the extracellular enzymatic machinery of the fungus to degrade lignin. The secreted, extracellular oxidase generates H2O2 for extracellular peroxidases
physiological function
-
the enzyme is part of the extracellular enzymatic machinery of the fungus to degrade lignin. The secreted, extracellular oxidase generates H2O2 for extracellular peroxidases. O2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of 4-methoxylated benzylic metabolites secreted by the fungus. AAO provides a continuous supply of H2O2 by redox cycling phenolic benzylic alcohol compounds, in collaboration with mycelium dehydrogenases
physiological function
-
the flavoenzyme aryl-alcohol oxidase is involved in lignin degradation
physiological function
-
the enzyme provides H2O2 to ligninolytic peroxidases
physiological function
-
aryl-alcohol oxidase is a flavoenzyme responsible for activation of O2 to H2O2 in fungal degradation of lignin
physiological function
-
aryl-alcohol oxidase (AAO) is an extracellular flavoprotein that supplies ligninolytic peroxidases with H2O2 during natural wood decay
physiological function
-
the aryl-alcohol oxidase acts on the lignin fraction in biomass
physiological function
the enzyme is involved in the degradation of 5-hydroxymethylfurfural. Two enzymes groups, which belong to the ligninolytic system, aryl-alcohol oxidase and a dehydrogenase, are involved in this process
physiological function
-
aryl-alcohol oxidase generates H2O2 for lignin degradation at the expense of benzylic and other Pi system-containing primary alcohols, which are oxidized to the corresponding aldehydes; the enzyme is involved in lignin degradation. Within this multienzymatic process, which enables the recycling of carbon fixed by photosynthesis in land ecosystems, AAO reduces O2, providing the H2O2 required by ligninolytic peroxidases to oxidize the recalcitrant lignin polymer
physiological function
-
the enzyme is involved in the degradation of 5-hydroxymethylfurfural. Two enzymes groups, which belong to the ligninolytic system, aryl-alcohol oxidase and a dehydrogenase, are involved in this process
-
additional information
-
structure-function relationship and analysis, overview. His502 activates the alcohol substrate by proton abstraction. Alcohol docking at the buried AAO active site results in only one catalytically relevant position for concerted transfer, with the pro-R alpha-hydrogen at distance for hydride abstraction, the enzyme shows hydride-transfer stereoselectivity
additional information
mixed quantum mechanics/molecular mechanics studies and molecular dynamics, overview
additional information
-
docking of 4-methoxybenzyl alcohol at the buried crystal active site, and quantum mechanical/molecular mechanical study, overview
additional information
-
AAO shows a buried active site connected to the solvent by a hydrophobic funnel-shaped channel, with Phe501 and two other aromatic residues forming a narrow bottleneck that prevents the direct access of alcohol substrates, while O2 has access to the active site following this channel. The side chain of Phe501, contiguous to the catalytic His502 in AAO, helps to position O2 at an adequate distance from flavin C4a (and His502Nepsilon). Phe501 substitution with a bulkier tryptophan residue results in an increase in theO2 reactivity of this flavoenzyme, free diffusion simulations of O2 inside the active-site cavity of AAO, the O2 reactivity of AAO decreases when the access channel is enlarged and increases when it is constricted by introducing a tryptophan residue, overview
additional information
-
residue 91 lies in the flavin attachment loop motif, and it is a highly conserved residue in all members of the GMC superfamily as Asn91, except for Pleurotus eryngii and Pleurotus pulmonarius AAO
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
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
-
-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
-
mutant F501A
-
-
?
1-naphthalene methanol + O2
alpha-naphthaldehyde + H2O2
-
27% of the activity with cinnamyl alcohol
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
-
50% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 75% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
-
-
?
2,5-hydroxymethylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
-
very low activity
-
-
?
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
-
?
3,5-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-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-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-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
-
7.6% of the activity with anisyl alcohol
-
-
?
5-hydroxymethylfurfural + O2
2,5-hydroxymethylfurancarboxylic acid + 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
-
?
veratryl alcohol + 2,6-dichlorophenol indophenol
veratrylaldehyde + red. 2,6-dichlorophenol indophenol
-
-
-
-
?
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-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
177.5% of the activity with benzyl alcohol
-
?
2,4-hexadien-1-ol + O2
? + H2O2
-
531% of the activity with benzyl alcohol
-
?
2,5-diformylfuran + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
?
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-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-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-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
-
ping-pong mechanism
-
-
?
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
-
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-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-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
-
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
-
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
-
-
?
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
-
-
?
benzyl alcohol + O2
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
-
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-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
-
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
-
-
?
N-phenyl-1-naphthalenamine + O2
?
-
degradation, complete removal from soil
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
?
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
2,6-dichloroaniline + O2
?
-
degradation, complete removal from soil
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
O94219
the substrate is an extracellular fungal metabolite
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
-
r
7H-benz[DE]anthracen-7-one + O2
?
-
degradation, partial removal from soil
-
-
?
9,10-anthracenedione + O2
?
-
degradation, partial removal from soil
-
-
?
N-phenyl-1-naphthalenamine + O2
?
-
degradation, complete removal from soil
-
-
?
2,5-diformylfuran + O2
2,5-furandicarboxylic acid + H2O2
E5CZV8
-
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
B4F335
essential for the activation of the plant derived precursor salicin
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
B4F334
essential for the activation of the plant derived precursor salicin
-
-
?
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
O94219
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
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
-
-
?
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
?
-
-
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
?
-
O94219
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
FAD
-
the FAD-binding domain composed of four separate subregions, containing the ADP-binding betaalphabeta motif that is not only characteristic for the GMC oxidoreductases but conserved among many FAD-binding proteins
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Pleurotus laciniatocrenatus
-
no activation or induction by supplementation of CuSO4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-methoxybenzylamine
-
uncompetitive, pH-dependent inhibition, best at pH 8.0
2-hydroxybenzyl alcohol
substrate inhibition at concentrations of about 250 mM
2-hydroxybenzyl alcohol
substrate inhibition at concentrations of about 250 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Pleurotus laciniatocrenatus
-
enzyme is induced by glucose depletion, no activation or induction by supplementation of vanillic acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
2,4-hexadienal
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
3
3,4-difluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.7
3-chloro-4-anisaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
1.5
3-Chlorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
2.2
3-Fluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
4.7
4-Chlorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
4.9
4-Fluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
7
benzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
8
veratraldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.092
2,4-hexadien-1-ol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.12
2,4-hexadien-1-ol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
2.88
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.269
3-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.293
3-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
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
0.028
4-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.037
4-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
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
0.029
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, wild-type enzyme, overall reaction
0.046
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, mutant F501W, oxidative half-reaction
0.049
4-methoxybenzyl alcohol
-
substrate 4-methoxybenzyl alcohol, pH 6.0, 25°C
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
1.08
4-methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
3.6
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, mutant F501A, oxidative half-reaction
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
0.758
benzyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.873
benzyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
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
additional information
additional information
-
stopped-flow and steady-state kinetics
-
additional information
additional information
-
steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview
-
additional information
additional information
-
Michaelis–Menten kinetics and redox potentials of wild-type and mutant enzymes, 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
Michaelis-Menten steady-state and transient-state kinetics of wild-type and mutant enzymes, overview
-
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
-
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
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state and stopped-flow kinetics, bi-substrate kinetics analysis, kinetic mechanisms, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
2,4-hexadienal
-
wild type enzyme, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.867
3,4-difluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.057
3-chloro-4-anisaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.85
3-Chlorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.883
3-Fluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
115.4
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
1.05
4-Chlorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.367
4-Fluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.5
benzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.13
veratraldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
105.7
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.012
4-anisaldehyde
-
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.05
4-anisaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
25
4-methoxybenzyl alcohol
-
substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C
105
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, wild-type enzyme, overall reaction
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
2,4-hexadienal
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.282
3,4-difluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
39.7
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.085
3-chloro-4-anisaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.643
3-Chlorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.407
3-Fluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
23.5
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.223
4-Chlorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.075
4-Fluorobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.073
benzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.0167
veratraldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.013
4-anisaldehyde
-
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.087
4-anisaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
11
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, mutant F501A, oxidative half-reaction
483
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, mutant F501Y, oxidative half-reaction
784
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, wild-type enzyme, oxidative half-reaction
1020
4-methoxybenzyl alcohol
-
substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C
1390
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, mutant F501W, oxidative half-reaction
3620
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, wild-type enzyme, overall reaction
3980
4-methoxybenzyl alcohol
-
substrate 4-methoxybenzyl alcohol, pH 6.0, 25°C
5120
4-methoxybenzyl alcohol
-
pH 6.0, 25°C, mutant F501Y, overall reaction
0.315
4-Nitrobenzaldehyde
-
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.597
4-Nitrobenzaldehyde
-
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.155
-
crude enzyme, using veratryl alcohol as substrate, at pH 6.0, 40°C
1.58
-
after 10.19fold purification, using veratryl alcohol as substrate, at pH 6.0, 40°C
additional information
additional information
cloning and microsequencing of peptides, substrate specificity of recombinant and native enzyme, phylogeny and comparison of sequence similarities
additional information
-
cloning and microsequencing of peptides, substrate specificity of recombinant and native enzyme, phylogeny and comparison of sequence similarities
additional information
cloning and microsequencing of peptides, substrate specificity of recombinant in comparison with native enzyme, phylogeny and comparison of sequence similarities
additional information
-
cloning and microsequencing of peptides, substrate specificity of recombinant in comparison with native enzyme, phylogeny and comparison of sequence similarities
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
3 - 7
the enzyme shows more than 90% of maximal activity, measured at pH 5.0, in the pH range between pH 4 and pH 6 and more than 80% between pH 3 and pH 7
3.5 - 8
-
pH 3.5: about 70% of maximal activity, pH 8.0: about 65% of maximal activity
4 - 9
-
AAO shows no pH dependence of kcat or catalytic efficiency for the substrates analyzed, AAO is unstable above pH 9.0