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Information on EC 1.1.3.7 - aryl-alcohol oxidase
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1.1.3.7 aryl-alcohol oxidaseIUBMB Comments
Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
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Word Map
- 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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film
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porous
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nanostructures
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aorta
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ascending
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nanotube
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nanowires
- lignin
- laccase
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decolor
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ophthalmology
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nanorods
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age-at-onset
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academy
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ligninolytic
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nanochannels
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etch
- pleurotus
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white-rot
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free-standing
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bicuspid
- eryngii
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electrodeposition
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sputter
- environmental protection
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valsalva
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four-dimensional
- synthesis
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president
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glucose-methanol-choline
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large-area
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template-assisted
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aortopathy
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nanopillars
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polycrystalline
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remazol
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nanopatterns
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photovoltaic
- bjerkandera
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nanoarrays
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
AAO, alcohol: O2 oxidoreductase, AOX, arom. alcohol oxidase, aryl alcohol oxidase, arylalcohol oxidase, CpSAO, CtSAO, More, MtGloA, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAO
alcohol: O2 oxidoreductase
AOX
arom. alcohol oxidase
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aryl alcohol oxidase
oxidase, aryl alcohol
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salicyl alcohol oxidase
VAO
veratryl alcohol oxidase
additional information
AAO
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-
-
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AAO
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aryl alcohol oxidase
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VAO
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veratryl alcohol oxidase
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additional information
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the enzyme belongs to the glucose-methanol-choline oxidoreductases, GMC, family
additional information
the enzyme belongs to the the glucose-methanol-choline oxidase, GMC, family of oxidoreductases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
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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
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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
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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
oxidation mechanism by AAO, 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
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9028-77-7
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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
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-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
mutant F501A
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-
?
1-naphthalene methanol + O2
alpha-naphthaldehyde + H2O2
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27% of the activity with cinnamyl alcohol
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-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
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50% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 75% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
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-
?
2-methoxybenzyl alcohol + O2
2-methoxybenzaldehyde + H2O
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23% of the activity with 2-hydroxybenzyl alcohol
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?
2-naphthalenemethanol + O2
2-naphthaleneformaldehyde + H2O
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745.7% of the activity with benzyl alcohol
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?
3,4-difluorobenzaldehyde + O2
3,4-difluorobenzoic acid + H2O2
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-
-
r
3,5-dimethoxybenzyl alcohol + O2
3,5-dimethoxy benzaldehyde + H2O2
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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
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high activity
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?
3-chloro-4-methoxybenzyl alcohol + O2
3-chloro-4-methoxybenzaldehyde + H2O2
ternary mechanism
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?
3-fluorobenzyl alcohol + O2
3-fluorobenzyl aldehyde + H2O2
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low activity
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?
3-hydroxy-4-methoxybenzyl alcohol + O2
3-hydroxy-4-methoxybenzaldehyde + H2O2
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62% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 71% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
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-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzylaldehyde + H2O
recombinant enzyme shows 1% of the activity with 2-hydroxybenzyl alcohol
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-
?
3-phenoxybenzyl alcohol + O2
3-phenoxybenzaldehyde + H2O2
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35% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 18% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
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?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
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7.6% of the activity with anisyl alcohol
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-
?
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
-
-
-
r
5-(hydroxymethyl)furan-2-carboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
very low activity
-
-
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
-
-
?
coniferyl alcohol + O2
coniferyl aldehyde + H2O2
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13% of the activity with cinnamyl alcohol
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-
?
cyclohexyl alcohol + O2
cyclohexyl aldehyde + H2O2
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12% of the activity with cinnamyl alcohol
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?
Direct Red 5B + O2
3-diazenyl-7-[(phenylcarbonyl)amino]naphthalene-2-sulfonic acid + H2O2
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degradation, dye decolorizing
product identification by GC-MS analysis
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?
veratryl alcohol + 2,6-dichlorophenol indophenol
veratrylaldehyde + red. 2,6-dichlorophenol indophenol
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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
?
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degradation, partial removal from soil
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?
1,2,3,4-tetrachlorobenzene + O2
?
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degradation, complete removal from soil
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?
1,2,4,5-tetrachlorobenzene + O2
?
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degradation, complete removal from soil
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?
1,2-binaphthalene + O2
?
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degradation, partial removal from soil
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?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
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degradation, partial removal from soil
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?
1-amino-9,10-anthracenedione + O2
?
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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
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r
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
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177.5% of the activity with benzyl alcohol
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?
2,4-hexadien-1-ol + O2
? + H2O2
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531% of the activity with benzyl alcohol
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?
2,6-dichloroaniline + O2
?
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degradation, complete removal from soil
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
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i.e. salicyl alcohol
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
i.e. salicyl alcohol
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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
i.e. salicyl alcohol
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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
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i.e. salicyl alcohol
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?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
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14% of the activity with 2-hydroxybenzyl alcohol
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?
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
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?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
recombinant enzyme shows 2.3% of the activity with 2-hydroxybenzyl alcohol
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?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
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21% of the activity with 2-hydroxybenzyl alcohol
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?
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
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?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
recombinant enzyme shows 21.9% of the activity with 2-hydroxybenzyl alcohol
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?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
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r
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
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21% of the activity with 2-hydroxybenzyl alcohol
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?
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
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?
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
recombinant enzyme shows 1.2% of the activity with 2-hydroxybenzyl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
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326.1% of the activity with benzyl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
ternary mechanism
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-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
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5.6% of the activity with 4-methoxybenzyl alcohol
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-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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31% of the activity with cinnamyl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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7.6% of the activity with anisyl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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at 63% of the activity with 3-methoxybenzyl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
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i.e. veratryl alcohol
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?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
ping-pong mechanism
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-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
ping-pong mechanism
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-
?
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
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-
?
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
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60% of the activity with cinnamyl alcohol
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-
?
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
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-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
-
-
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?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
as active as benzyl alcohol
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?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
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32% of the activity with 4-methoxybenzyl alcohol
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
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
-
-
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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
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-
?
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
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-
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
-
-
?
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
?
-
-
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
?
-
-
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 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
-
-
?
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
-
-
?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
-
-
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
r
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + 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-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
-
-
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
essential for the activation of the plant derived precursor salicin
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
high activity, 4-methoxybenzyl alcohol, is one of the best substrates of AAO, and 4-methoxybenzaldehyde (4-anisaldehyde) is the main extracellular aromatic metabolite in Pleurotus species
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
i.e. 4-anisyl alcohol
-
-
?
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
?
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
-
AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
-
-
?
additional information
?
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid
-
-
?
additional information
?
-
the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
-
-
?
additional information
?
-
-
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Pleurotus laciniatocrenatus
-
no activation or induction by supplementation of CuSO4
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INHIBITOR
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
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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
-
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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
0.025
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant wild-type enzyme
0.029
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, overall reaction
0.035
4-methoxybenzyl alcohol
-
recombinant wild-type enzyme, pH 6.0, 24°C
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
0.051
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant mutant Y92L
0.134
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, oxidative half-reaction
0.167
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
0.18
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, oxidative half-reaction
0.249
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
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
0.017
O2
with 3-fluorobenzyl alcohol, 25°C, pH 6.0, recombinant enzyme
0.541
veratryl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.59 - 1
veratryl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
stopped-flow and steady-state kinetics
-
additional information
additional information
-
MichaelisâMenten kinetics and redox potentials of wild-type and mutant enzymes, overview
-
additional information
additional information
steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview
-
additional information
additional information
mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base
-
additional information
additional information
-
mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base
-
additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of overall and half-reactions of wild-type and mutant enzymes by (anaerobic) stopped-flow spectrophotometry, changes in the flavin redox state, detailed overview
-
additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady state and transient state kinetic constants for alcohol and O2 of AAO oxidation of a deuterated and normal (alpha-protiated) 4-methoxybenzyl alcohol, solvent kinetic isotope effects, overview
-
additional information
additional information
steady-state and transient kinetics of overall reaction, and oxidative and reductive half-reactions, overview
-
additional information
additional information
steady-state and stopped-flow kinetics, bi-substrate kinetics analysis, kinetic mechanisms, overview
-
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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
40
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
64
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
87
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, overall reaction
105
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, overall reaction
129
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant wild-type enzyme
140.9
4-methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
196
4-methoxybenzyl alcohol
substrate 4-methoxybenzyl alcohol, pH 6.0, 25°C
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
240
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, overall reaction
257
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
483
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501Y, oxidative half-reaction
784
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, oxidative half-reaction
1020
4-methoxybenzyl alcohol
substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C
1390
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, oxidative half-reaction
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
5160
4-methoxybenzyl alcohol
pH 6.0, 12°C, recombinant wild-type enzyme
0.315
4-nitrobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.597
4-nitrobenzaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
6 - 6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 - 9
3.5 - 8
-
pH 3.5: about 70% of maximal activity, pH 8.0: about 65% of maximal activity
4 - 7
-
the enzyme displays over 63% of its activity in the pH range of 4.0-7.0. A further increase of these pH values decreases the relative activity to 17%
4 - 9
AAO shows no pH dependence of kcat or catalytic efficiency for the substrates analyzed, AAO is unstable above pH 9.0
5.3 - 7.3
-
pH 5.3: about 90% of maximal activity, pH 7.3: 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
20°C: about 55% of maximal activity, 60°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
