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Information on EC 1.1.3.7 - aryl-alcohol oxidase
for references in articles please use BRENDA:EC1.1.3.7
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.7 aryl-alcohol oxidase
IUBMB Comments
Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.3.7
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anodic
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aluminum
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fabric
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nanoporous
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porous
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film
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nanostructures
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ascending
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aorta
- lignin
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nanowires
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nanotube
- laccase
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etch
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nanochannels
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ophthalmology
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age-at-onset
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academy
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decolor
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nanorods
- pleurotus
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ligninolytic
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white-rot
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bicuspid
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free-standing
- eryngii
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electrodeposition
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sputter
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valsalva
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large-area
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template-assisted
- environmental protection
- synthesis
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aortopathy
- bjerkandera
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nanopillars
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four-dimensional
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nanopatterns
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photovoltaic
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polycrystalline
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remazol
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glucose-methanol-choline
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president
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nanoarrays
showSynonyms
aao, aryl-alcohol oxidase, veratryl alcohol oxidase, aryl alcohol oxidase, salicyl alcohol oxidase, arylalcohol oxidase, mtgloa, cpsao, 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
GaoB
GLRG_02805
GMC oxidoreductase-like protein
HMFO
MYCTH_2299749
oxidase, aryl alcohol
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salicyl alcohol oxidase
VAO
veratryl alcohol oxidase
additional information
AAO
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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, 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
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
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
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
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
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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-3-phenylprop-2-en-1-ol + O2
(2E)-3-phenylprop-2-enal + H2O2
Substrates: -
Products: -
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?
(2E)-hept-2-en-1-ol + O2
(2E)-hept-2-enal + H2O2
Substrates: 31.9% of the activity with benzyl alcohol
Products: -
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?
(2E,4E)-hepta-2,4-dien-1-ol + O2
(2E,4E)-hepta-2,4-dienal + H2O2
Substrates: 737% of the activity with benzyl alcohol
Products: -
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?
(2E,4E)-hexa-2,4-dien-1-ol + O2
(2E,4E)-hexa-2,4-dienal + H2O2
Substrates: 807% of the activity with benzyl alcohol
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?
(2E,4E)-hexa-2,4-dien-1-ol + O2
? + H2O2
Substrates: 282% of the activity with benzyl alcohol
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?
(2H-1,3-benzodioxol-5-yl)methanol + O2
2H-1,3-benzodioxole-5-carbaldehyde + H2O2
Substrates: 301% of the activity with benzyl alcohol
Products: -
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?
(2R,3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-ol + O2
(3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one + H2O2
Substrates: 4% conversion, 2% enantiomeric excess
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?
(2R,3E)-4-(4-chlorophenyl)but-3-en-2-ol + O2
(3E)-4-(4-chlorophenyl)but-3-en-2-one + H2O2
Substrates: 10% conversion, 10% enantiomeric excess
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?
(2R,3E)-4-(4-methylphenyl)but-3-en-2-ol + O2
(3E)-4-(4-methylphenyl)but-3-en-2-one + H2O2
Substrates: 13% conversion, 14% enantiomeric excess
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(2R,3E)-4-phenylbut-3-en-2-ol + O2
(3E)-4-phenylbut-3-en-2-one + H2O2
Substrates: 29% conversion, 25% enantiomeric excess
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?
(2R,3E)-oct-3-en-2-ol + O2
(3E)-oct-3-en-2-one + H2O2
Substrates: 16% conversion, 19% enantiomeric excess
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?
(naphthalen-2-yl)methanol + O2
naphthalene-2-carbaldehyde + H2O2
Substrates: 874% of the activity with benzyl alcohol
Products: -
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?
(pyrene-1-yl)methanol + O2
pyrene-1-carbaldehyde + H2O2
Substrates: 35% of the activity with benzyl alcohol
Products: -
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?
(S)-1-(4-methoxyphenyl)-ethanol + O2
1-(4-methoxyphenyl)acetaldehyde + H2O2
Substrates: -
Products: -
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?
(thiophen-2-yl)methanol + O2
thiophene-2-carbaldehyde + H2O2
Substrates: 15.8% of the activity with benzyl alcohol
Products: -
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?
1-naphthalene methanol + O2
alpha-naphthaldehyde + H2O2
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Substrates: 27% of the activity with cinnamyl alcohol
Products: -
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?
2,4-hexadien-1-ol + 2 O2
2,4-hexadienal + 2 H2O2
Substrates: -
Products: -
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?
2,4-hexadien-1-ol + O2
2,4-hexandienal + H2O2
-
Substrates: -
Products: -
Products: -
?
2,4-hexadienal + O2
2,4-hexadienoate + H2O2
Substrates: -
Products: -
Products: -
?
2,5-diformylfuran + 2 O2
2,5-furandicarboxylic acid + H2O2
Substrates: -
Products: -
Products: -
ir
2,5-diformylfuran + O2
formylfurancarboxylic acid + ?
Substrates: -
Products: -
Products: -
?
2-anisyl alcohol + O2
2-anisyl aldehyde + H2O2
Substrates: 96% of the activity with benzyl alcohol
Products: -
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?
2-methoxybenzyl alcohol + O2
2-methoxybenzaldehyde + H2O
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Substrates: 23% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
2-naphthalenemethanol + O2
2-naphthaleneformaldehyde + H2O
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Substrates: 745.7% of the activity with benzyl alcohol
Products: -
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?
3,4-difluorobenzaldehyde + O2
3,4-difluorobenzoic acid + H2O2
Substrates: -
Products: -
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?, r
3,5-dimethoxybenzyl alcohol + O2
3,5-dimethoxy benzaldehyde + H2O2
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Substrates: 7% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 8% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
Products: -
?
3-anisyl alcohol + O2
3-anisaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
3-chloro-4-anisaldehyde + O2
3-chloro-4-anisic acid + H2O2
Substrates: -
Products: -
Products: -
r
3-chloro-4-anisyl alcohol + O2
3-chloro-4-anisaldehyde + H2O2
Substrates: -
Products: -
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?
3-chloro-4-anisyl alcohol + O2
3-chloro-4-anisyl aldehyde + H2O2
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Substrates: high activity
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?
3-chloro-4-methoxybenzyl alcohol + O2
3-chloro-4-methoxybenzaldehyde + H2O2
Substrates: ternary mechanism
Products: -
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?
3-chlorobenzaldehyde + O2
3-chlorobenzoic acid + H2O2
Substrates: -
Products: -
Products: -
r
3-chlorobenzyl alcohol + O2
3-chlorobenzyl aldehyde + H2O2
-
Substrates: -
Products: -
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?
3-fluorobenzaldehyde + O2
3-fluorobenzoic acid + H2O2
Substrates: -
Products: -
Products: -
r
3-fluorobenzyl alcohol + O2
3-fluorobenzyl aldehyde + H2O2
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Substrates: low activity
Products: -
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?
3-hydroxy-4-methoxybenzyl alcohol + O2
3-hydroxy-4-methoxybenzaldehyde + H2O2
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Substrates: 62% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 71% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
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?
3-methoxybenzyl alcohol + O2
3-methoxybenzylaldehyde + H2O2
Substrates: recombinant enzyme shows 1% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
3-phenoxybenzyl alcohol + O2
3-phenoxybenzaldehyde + H2O2
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Substrates: 35% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 18% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
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?
4-aminobenzyl alcohol + O2
4-aminobenzaldehyde + H2O2
Substrates: 18.6% of the activity with benzyl alcohol
Products: -
Products: -
?
4-chlorobenzaldehyde + O2
4-chlorobenzoic acid + H2O2
Substrates: -
Products: -
Products: -
r
4-chlorobenzyl alcohol + O2
4-chlorobenzyl aldehyde + H2O2
-
Substrates: -
Products: -
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?
4-fluorobenzaldehyde + O2
4-fluorobenzoic acid + H2O2
Substrates: -
Products: -
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r
4-fluorobenzyl alcohol + O2
4-fluorobenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-fluorobenzyl alcohol + O2
4-fluorobenzyl aldehyde + H2O2
-
Substrates: -
Products: -
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?
4-methoxybenzyl alcohol + O2
4-methoxybenzyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
Substrates: -
Products: -
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r
4-nitrobenzaldehyde + O2
4-nitrobenzoic acid + H2O2
Substrates: -
Products: -
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?, r
4-nitrobenzyl alcohol + O2
4-nitrobenzaldehyde + H2O2
Substrates: -
Products: -
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r
5-(hydroxymethyl)furan-2-carboxylic acid + O2
2,5-furandicarboxylic acid + ?
Substrates: very low activity
Products: -
Products: -
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
5-formylfuran-2-carboxylic acid + H2O2
Substrates: -
Products: -
Products: -
?
coniferyl alcohol + O2
coniferyl aldehyde + H2O2
-
Substrates: 13% of the activity with cinnamyl alcohol
Products: -
Products: -
?
cumic alcohol + O2
cumic aldehyde + H2O2
Substrates: 149% of the activity with benzyl alcohol
Products: -
Products: -
?
cyclohexyl alcohol + O2
cyclohexyl aldehyde + H2O2
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Substrates: 12% of the activity with cinnamyl alcohol
Products: -
Products: -
?
ethanol + O2
acetaldehyde + H2O2
-
Substrates: low activity
Products: -
Products: -
?
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
Substrates: -
Products: -
Products: -
?
vanillyl alcohol + O2
vanillyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratraldehyde + O2
veratric acid + H2O2
Substrates: -
Products: -
Products: -
r
veratryl alcohol + 2,6-dichlorophenol indophenol
veratrylaldehyde + red. 2,6-dichlorophenol indophenol
-
Substrates: -
Products: -
Products: -
?
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
Substrates: 63.9% of the activity with benzyl alcohol
Products: -
Products: -
?
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
Substrates: -
Products: -
Products: -
?
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
-
Substrates: -
Products: -
Products: -
?
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
Substrates: over 98% excess of the R enantiomer after treatment of racemic 1-(4-methoxyphenyl)ethanol, the hydride transfer is highly stereoselective
Products: -
Products: -
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
Substrates: mutant F501A
Products: -
Products: -
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
1,1'-binaphthalene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1,2,3,4,5-pentachlorobenzene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1,2,3,4,5-pentachlorobenzene + O2
?
-
Substrates: very low activity
Products: -
Products: -
?
1,2,3,4-tetrachlorobenzene + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
1,2,3,4-tetrachlorobenzene + O2
?
-
Substrates: high activity
Products: -
Products: -
?
1,2,4,5-tetrachlorobenzene + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
1,2,4,5-tetrachlorobenzene + O2
?
-
Substrates: high activity
Products: -
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?
1,2-binaphthalene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
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?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
Substrates: -
Products: -
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?
1-amino-9,10-anthracenedione + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
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?
1-amino-9,10-anthracenedione + O2
?
-
Substrates: lower activity
Products: -
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?
1-chloro-9,10-anthracenedione + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1-chloro-9,10-anthracenedione + O2
?
-
Substrates: very low activity
Products: -
Products: -
?
2,4-dichloroaniline + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
Substrates: 177.5% of the activity with benzyl alcohol
Products: -
Products: -
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
Substrates: 286% of the activity with benzyl alcohol
Products: -
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?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzyl aldehyde + H2O2
-
Substrates: 50% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 75% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
Products: -
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
-
Substrates: high activity
Products: -
Products: -
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
Substrates: -
Products: -
Products: -
?
2,4-hexadien-1-ol + O2
2,4-hexadienal + H2O2
Substrates: -
Products: -
Products: -
?
2,4-hexadien-1-ol + O2
? + H2O2
-
Substrates: 531% of the activity with benzyl alcohol
Products: -
Products: -
?
2,5-diformylfuran + O2
5-formylfuran-2-carboxylic acid + ?
Substrates: -
Products: -
Products: -
?
2,5-diformylfuran + O2
5-formylfuran-2-carboxylic acid + ?
Substrates: -
Products: -
Products: -
?
2,6-dichloroaniline + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
-
Substrates: i.e. salicyl alcohol
Products: -
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: essential for the activation of the plant derived precursor salicin
Products: -
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: i.e. salicyl alcohol
Products: -
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: essential for the activation of the plant derived precursor salicin
Products: -
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: i.e. salicyl alcohol
Products: -
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?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
-
Substrates: i.e. salicyl alcohol
Products: -
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?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
-
Substrates: 14% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
Substrates: recombinant enzyme shows 3.2% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 14% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
2-methoxybenzyl alcohol + O2
2-methoxybenzylaldehyde + H2O
Substrates: recombinant enzyme shows 2.3% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
-
Substrates: 21% of the activity with 2-hydroxybenzyl alcohol
Products: -
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2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
Substrates: recombinant enzyme shows 19.1% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 21% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
2-methylbenzyl alcohol + O2
2-methylbenzylaldehyde + H2O
Substrates: recombinant enzyme shows 21.9% of the activity with 2-hydroxybenzyl alcohol
Products: -
Products: -
?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
Substrates: best substrate
Products: -
Products: -
r
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
-
Substrates: 21% of the activity with 2-hydroxybenzyl alcohol
Products: -
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?
2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
Substrates: recombinant enzyme shows 3.8% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 21% of the activity with 2-hydroxybenzyl alcohol
Products: -
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2-phenylethyl alcohol + O2
2-phenylacetaldehyde + H2O
Substrates: recombinant enzyme shows 1.2% of the activity with 2-hydroxybenzyl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
-
Substrates: 326.1% of the activity with benzyl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
Substrates: ternary mechanism
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
-
Substrates: 5.6% of the activity with 4-methoxybenzyl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: 31% of the activity with cinnamyl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: 7.6% of the activity with anisyl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: at 63% of the activity with 3-methoxybenzyl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: i.e. veratryl alcohol
Products: -
Products: -
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
Substrates: 297% of the activity with benzyl alcohol
Products: -
Products: -
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
3-anisyl alcohol + O2
3-anisyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
Substrates: ping-pong mechanism
Products: -
Products: -
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
Substrates: ping-pong mechanism
Products: -
Products: -
?
3-hydroxybenzyl alcohol + O2
3-hydroxybenzaldehyde + H2O2
Substrates: 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
Products: -
Products: -
?
3-hydroxybenzyl alcohol + O2
3-hydroxybenzaldehyde + H2O2
Substrates: recombinant enzyme shows 16.2% of the activity with 2-hydroxybenzyl alcohol
Products: -
Products: -
?
3-hydroxybenzyl alcohol + O2
3-hydroxybenzaldehyde + H2O2
Substrates: 221% of the activity with benzyl alcohol
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
Substrates: 60% of the activity with cinnamyl alcohol
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
Substrates: i.e. 3-anisyl alcohol
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
Substrates: i.e. 3-anisyl alcohol
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
Substrates: 19% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 16% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
Substrates: as active as benzyl alcohol
Products: -
Products: -
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
Substrates: 32% of the activity with 4-methoxybenzyl alcohol
Products: -
Products: -
?
4-anisaldehyde + O2
4-anisic acid + H2O2
Substrates: -
Products: -
Products: -
r
4-anisaldehyde + O2
4-anisic acid + H2O2
Substrates: -
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
Substrates: the substrate is an extracellular fungal metabolite
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
Substrates: best substrate
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
r
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
Substrates: 298% of the activity with benzyl alcohol
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
-
Substrates: best substrate
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
Substrates: preferred substrate
Products: -
Products: -
?
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-chlorobenzyl alcohol + O2
4-chlorobenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
Substrates: 15% of the activity with anisyl alcohol
Products: -
Products: -
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
Substrates: 12% of the activity with 4-methoxybenzyl alcohol
Products: -
Products: -
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
Substrates: recombinant enzyme shows 2.7% of the activity with 2-hydroxybenzyl alcohol
Products: -
Products: -
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
-
Substrates: 7.6% of the activity with anisyl alcohol
Products: -
Products: -
?
4-hydroxybenzyl alcohol + O2
4-hydroxybenzyl aldehyde + H2O2
Substrates: 207% of the activity with benzyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: 63% of the activity with cinnamyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: i.e. 4-anisyl alcohol, best substrate
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: i.e. 4-anisyl alcohol, best substrate
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: 200% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 266% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: 15% of the activity with 3-methoxybenzyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: 571.4% of the activity with benzyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: 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
Products: -
Products: -
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: ternary mechanism
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
furan-2,5-dicarboxylic acid + ?
Substrates: -
Products: -
Products: -
?
5-(hydroxymethyl)furan-2-carboxylic acid + O2
furan-2,5-dicarboxylic acid + ?
Substrates: -
Products: -
Products: -
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
5-(hydroxymethyl)furfural + O2
furan-2,5-dicarbaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
Substrates: -
Products: -
Products: -
?
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
5-formylfuran-2-carboxylate + O2
furan-2,5-dicarboxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + 5-formylfuran-2-carboxylic acid + H2O2
Thermothelomyces thermophilus DSM 1799
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-furandicarboxylic acid + ?
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
2,5-furandicarboxylic acid + ?
-
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
Substrates: -
Products: -
Products: -
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
Substrates: -
Products: -
Products: -
?
7H-benz[DE]anthracen-7-one + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
7H-benz[DE]anthracen-7-one + O2
?
-
Substrates: low activity
Products: -
Products: -
?
9,10-anthracenedione + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
anisyl alcohol + O2
anisaldehyde + H2O2
-
Substrates: best substrate
Products: -
Products: -
?
anisyl alcohol + O2
anisaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
anisyl alcohol + O2
anisaldehyde + H2O2
Substrates: best substrate
Products: -
Products: -
?
anisyl alcohol + O2
anisaldehyde + H2O2
Substrates: best substrate
Products: -
Products: -
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
Substrates: 647% of the activity with benzyl alcohol
Products: -
Products: -
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
Thermothelomyces thermophilus DSM 1799
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: 26% of the activity with cinnamyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: poorest substrate
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: poorest substrate
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: 5.0% of the activity with anisyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: recombinant enzyme shows 12.2% of the activity with 2-hydroxybenzyl alcohol, native enzyme shows 23% of the activity with 2-hydroxybenzyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: recombinant enzyme shows 23.2% of the activity with 2-hydroxybenzyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: 30% of the activity with 3,4-dimethoxybenzyl alcohol, VAO I. 25% of the activity with 3,4-dimethoxybenzyl alcohol, VAO II
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: 19% conversion
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: at 28% of the activity with 3-methoxybenzyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, overview
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: 3.6% of the activity with 4-methoxybenzyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
benzyl alcohol + O2
benzyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
beta-naphthylcarbinol + O2
beta-naphthaldehyde + H2O2
-
Substrates: 80% of the activity with cinnamyl alcohol
Products: -
Products: -
?
beta-naphthylcarbinol + O2
beta-naphthaldehyde + H2O2
-
Substrates: 114% of the activity with 4-methoxybenzyl alcohol
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
Substrates: 451.1% of the activity with benzyl alcohol
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
Substrates: high activity
Products: -
Products: -
r
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + O2
cinnamic aldehyde + H2O2
-
Substrates: 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
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
Substrates: 289% of the activity with benzyl alcohol
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
Substrates: 442% of the activity with benzyl alcohol
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
Thermothelomyces thermophilus DSM 1799
Substrates: -
Products: -
Products: -
?
diphenylether + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
diphenylsulfone + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
Direct Red 5B + O2
3-diazenyl-7-[(phenylcarbonyl)amino]naphthalene-2-sulfonic acid + H2O2
-
Substrates: degradation, dye decolorizing
Products: product identification by GC-MS analysis
Products: product identification by GC-MS analysis
?
Direct Red 5B + O2
3-diazenyl-7-[(phenylcarbonyl)amino]naphthalene-2-sulfonic acid + H2O2
-
Substrates: degradation, dye decolorizing
Products: product identification by GC-MS analysis
Products: product identification by GC-MS analysis
?
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
furan-2,5-dicarbaldehyde + O2
5-formylfuran-2-carboxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
Substrates: 73% of the activity with benzyl alcohol
Products: -
Products: -
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
Substrates: 246% of the activity with benzyl alcohol
Products: -
Products: -
?
m-anisyl alcohol + O2
m-anisaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
N-phenyl-1-naphthalenamine + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
N-phenyl-1-naphthalenamine + O2
?
-
Substrates: high activity
Products: -
Products: -
?
n-propanol + O2
propionaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
naphthalene + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
Substrates: -
Products: -
Products: -
r
veratryl alcohol + O2
veratraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
Thermothelomyces thermophilus DSM 1799
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: 318% of the activity with benzyl alcohol
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: 322% of the activity with benzyl alcohol
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Pleurotus laciniatocrenatus
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
Substrates: i.e. 3,4-dimethoxybenzyl alcohol
Products: -
Products: -
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional enzyme showing aryl alcohol oxidase activity as well as secondary alcohol oxidase activity, EC 1.1.3.18, substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 3,4-dimethoxyphenyl acetic acid and 1-(3,4-dimethoxyphenyl)-2-phenylethanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
Products: -
Products: -
?
additional information
?
-
-
Substrates: belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
Products: -
Products: -
?
additional information
?
-
Substrates: belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
Products: -
Products: -
?
additional information
?
-
-
Substrates: belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline)
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is active on short-chain alkane diols and glycerol, and aryl alcohols, with similar specific activity values. Highest specific activity is observed on 5-hydroxymethylfurfural. Galactose and galactosylated oligosaccharides are poor substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is active on short-chain alkane diols and glycerol, and aryl alcohols, with similar specific activity values. Highest specific activity is observed on 5-hydroxymethylfurfural. Galactose and galactosylated oligosaccharides are poor substrates
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with mono- and disaccharides. No electron acceptor: DCIP
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with mono- and disaccharides. No electron acceptor: DCIP
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme displays weak activity on carbohydrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme displays weak activity on carbohydrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of H2O2 during oxidation of lignin fragments
Products: -
Products: -
?
additional information
?
-
Substrates: for sec-allylic alcohol substrates, exclusively oxidation of the allylic alcohol to the alpha,beta-unsaturated ketone is observed. The reaction is enantioselective for the R-enantiomer
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with aliphatic and secondary aromatic alcohols
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme provides H2O2 for fungal degradation of lignin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme provides H2O2 for fungal degradation of lignin
Products: -
Products: -
?
additional information
?
-
-
Substrates: 4-(hydroxymethyl)-benzoic acid is a poor substrate
Products: -
Products: -
?
additional information
?
-
Substrates: oxidation of aromatic and aliphatic polyunsaturated primary alcohols by wild-type and recombinant enzymes, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: oxidation of aromatic and aliphatic polyunsaturated primary alcohols by wild-type and recombinant enzymes, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: an H2O2-producing ligninolytic enzyme, molecular docking study of substrates, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: AAO typically oxidizes aromatic alcohols to the corresponding aldehydes. However, the enzyme can also oxidize aromatic aldehydes to the corresponding acids
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows a broad substrate specificity and highly stereoselective reaction mechanism. Assay method using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]/horseradish peroxidase
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: for complete oxidation of 5-hydroxymethylfurfural, the rate-limiting step lies in the final oxidation of the intermediate 5-formyl-furancarboxylic acid to 2,5-furandicarboxylic acid. Wild-type AAO is not able to catalyze 5-formyl-furancarboxylic acid oxidation
Products: -
Products: -
?
additional information
?
-
Pleurotus laciniatocrenatus
-
Substrates: a ligninolytic enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: decolorization of coal humic acid by the extracellular enzyme produced by white-rot fungi, low activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil, e.g. from chemical industrial sites, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, lignin-modifying enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview. No activity with caffeic acid
Products: -
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?
additional information
?
-
Substrates: no substrates: glucose, cellobiose, methanol
Products: -
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?
additional information
?
-
-
Substrates: no substrates: glucose, cellobiose, methanol
Products: -
Products: -
?
additional information
?
-
Thermothelomyces thermophilus DSM 1799
Substrates: no substrates: glucose, cellobiose, methanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
Substrates: over 98% excess of the R enantiomer after treatment of racemic 1-(4-methoxyphenyl)ethanol, the hydride transfer is highly stereoselective
Products: -
Products: -
?
1,1'-binaphthalene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
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?
1,2,3,4,5-pentachlorobenzene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1,2,3,4-tetrachlorobenzene + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
1,2,4,5-tetrachlorobenzene + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
1,2-binaphthalene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1-(2-naphthalenylmethyl)-naphthalene + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1-amino-9,10-anthracenedione + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
1-chloro-9,10-anthracenedione + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
2,4-dichloroaniline + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
2,5-diformylfuran + 2 O2
2,5-furandicarboxylic acid + H2O2
Substrates: -
Products: -
Products: -
ir
2,6-dichloroaniline + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
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?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
Substrates: best substrate
Products: -
Products: -
r
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
Substrates: the substrate is an extracellular fungal metabolite
Products: -
Products: -
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
Substrates: preferred substrate
Products: -
Products: -
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-hydroxybenzyl alcohol + O2
4-hydroxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
4-nitrobenzyl alcohol + O2
4-nitrobenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
r
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
Substrates: -
Products: -
Products: -
?
7H-benz[DE]anthracen-7-one + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
9,10-anthracenedione + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
Substrates: high activity
Products: -
Products: -
r
diphenylether + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
diphenylsulfone + O2
?
-
Substrates: degradation, partial removal from soil
Products: -
Products: -
?
N-phenyl-1-naphthalenamine + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
Products: -
?
naphthalene + O2
?
-
Substrates: degradation, complete removal from soil
Products: -
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?
veratryl alcohol + O2
veratryl aldehyde + H2O2
Pleurotus laciniatocrenatus
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratrylaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: essential for the activation of the plant derived precursor salicin
Products: -
Products: -
?
2-hydroxybenzyl alcohol + O2
2-hydroxybenzaldehyde + H2O2
Substrates: essential for the activation of the plant derived precursor salicin
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: -
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: 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
Products: -
Products: -
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
Substrates: i.e. 4-anisyl alcohol
Products: -
Products: -
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
n-propanol + O2
propionaldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
Substrates: -
Products: -
Products: -
r
veratryl alcohol + O2
veratraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
veratryl alcohol + O2
veratraldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of H2O2 during oxidation of lignin fragments
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme provides H2O2 for fungal degradation of lignin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme provides H2O2 for fungal degradation of lignin
Products: -
Products: -
?
additional information
?
-
-
Substrates: AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: decolorization of coal humic acid by the extracellular enzyme produced by white-rot fungi, low activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil, e.g. from chemical industrial sites, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ligninolytic activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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
Cu2+
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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-Hydroxybenzyl alcohol
-
shows substrate inhibition at higher concentration
4-methoxybenzylamine
-
uncompetitive, pH-dependent inhibition, best at pH 8.0
H2O2
inhibitory to the oxidation of formylfurancarboxylic acid, oxidation activities of AAO on 5-hydroxymethylfurfural and 2,5-diformylfuran are independent of the presence of H2O2
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
0.0204
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
0.0214
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C
0.0215
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)15(GGGGS)2, pH 4, 25°C
0.028
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C
0.0382
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C
0.092
2,4-hexadien-1-ol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.095
2,4-hexadien-1-ol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.096
2,4-hexadien-1-ol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.106
2,4-hexadien-1-ol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
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
0.022
4-methoxybenzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.023
4-methoxybenzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
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
0.028
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid
0.029
4-methoxybenzyl alcohol
pH 6.0, 25°C, wild-type enzyme, overall reaction
0.037
4-methoxybenzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
0.038
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid
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
3.1
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
26.9
5-(hydroxymethyl)furan-2-carboxylic acid
wild-type, pH 7, 25°C
27
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334F, pH 7, 25°C
42
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334W, pH 7, 25°C
0.37
benzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.38
benzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.44
benzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
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
0.34
veratryl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
0.36
veratryl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
0.41
veratryl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
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
-
MichaelisMenten kinetics and redox potentials 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
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 wild-type and mutant enzymes, 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
-
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
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
29
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C
30
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C
30
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C
34
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)15(GGGGS)2, pH 4, 25°C
44
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
47
2,4-hexadien-1-ol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
62
2,4-hexadien-1-ol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
89
2,4-hexadien-1-ol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
105.7
3,4-dimethoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
115.4
3-Methoxybenzyl 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
1.03
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid
1.32
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid
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
41
4-methoxybenzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
56.9
4-methoxybenzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
64
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501W, overall reaction
70
4-methoxybenzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
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
3.7
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334W, pH 7, 25°C
5.2
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
15.4
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334F, pH 7, 25°C
28.3
5-(hydroxymethyl)furan-2-carboxylic acid
wild-type, pH 7, 25°C
15.1
benzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
23.4
benzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
34.4
benzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
24.6
veratryl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
36.8
veratryl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
56.9
veratryl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
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
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
747
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C
1061
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C
1383
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C
1568
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (AP)15(GGGGS)2, pH 4, 25°C
2183
(R,S)-4-methoxybenzyl alcohol
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
456
2,4-hexadien-1-ol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
653
2,4-hexadien-1-ol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
840
2,4-hexadien-1-ol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
23.5
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
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
1782
4-methoxybenzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
1909
4-methoxybenzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
2080
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid
2250
4-methoxybenzyl alcohol
pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid
2586
4-methoxybenzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
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
0.088
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334W, pH 7, 25°C
0.57
5-(hydroxymethyl)furan-2-carboxylic acid
mutant Y334F, pH 7, 25°C
1.1
5-(hydroxymethyl)furan-2-carboxylic acid
wild-type, pH 7, 25°C
1.7
5-(hydroxymethyl)furan-2-carboxylic acid
pH 7.5, 25°C
41
benzyl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
62
benzyl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
78
benzyl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
72
veratryl alcohol
recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C
102
veratryl alcohol
recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C
139
veratryl alcohol
recombinant protein from wild-type Pichia pastoris, pH 6, 25°C
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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
0.2
-
recombinant protein, substrate vanillyl alcohol, reaction of EC 1.1.3.7, pH 7.0, 25°C
1.58
-
after 10.19fold purification, using veratryl alcohol as substrate, at pH 6.0, 40°C
3.3
recombinant protein, substrate vanillyl alcohol, pH 7.0, 25°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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 6.5
7.5
7.5 - 8
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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 - 10
5.3 - 7.3
-
pH 5.3: about 90% of maximal activity, pH 7.3: 35% of maximal activity
5.5
50% of the activity at pH 7.0, substrate 5-hydroxymethylfurfural
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
40
45
50
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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
4.5
isoelelctric focusing, recombinant protein from wild-type Pichia pastoris
4.6
isoelectric focusing, recombinant protein from glycosylation-deficient Saccharomyces cerevisiae
4.8
isoelectric focusing, recombinant protein from wild-type Saccharomyces cerevisiae
6.1
6.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
no activity in Fusarium oxysporum BAFC 738
-
solid-state culture
-
brenda
additional information
the enzyme is found in the hyphal sheath (formed by secreted polysaccharide) during wheat straw degradation by Pleurotus eryngii under solid-state fermentation conditions. The enzyme shows initial location on the hyphal surface, but can penetrate degraded cell walls of phloem and parenchyma, and also the more lignified sclerenchymatic tissues
brenda
additional information
-
the enzyme is found in the hyphal sheath (formed by secreted polysaccharide) during wheat straw degradation by Pleurotus eryngii under solid-state fermentation conditions. The enzyme shows initial location on the hyphal surface, but can penetrate degraded cell walls of phloem and parenchyma, and also the more lignified sclerenchymatic tissues
brenda
additional information
Pleurotus laciniatocrenatus
-
solid-state fermentation culture on Eucalyptus globulus wood chips
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme posseses a signal peptide, and it is secreted
-
brenda
-
the enzyme posseses a signal peptide, and it is secreted
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease 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 glucosemethanolcholine oxidase superfamily
evolution
the enzyme belongs to the glucose methanol choline oxidase superfamily
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 AA3_2 subfamily, phylogenetic analysis
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
metabolism
temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction. Kinetic isotope effects suggest an environmentally-coupled quantum-mechanical tunnelling process. AAO shows a preorganized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place
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 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
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 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
-
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 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
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
physiological function
Pleurotus ostreatus is capable to metabolize and detoxify 5-hydroxymethylfurfural at 30 mM within 48 h, converting it into 2,5-bis-hydroxymethylfuran and 2,5-furandicarboxylic acid. Two enzymes groups, which belong to the ligninolytic system, aryl-alcohol oxidases and a dehydrogenase, are involved in this process. 5-Hydroxymethylfurfural induces the transcription and production of these enzymes, accompanied by an increase in activity levels
physiological function
-
Pleurotus ostreatus is capable to metabolize and detoxify 5-hydroxymethylfurfural at 30 mM within 48 h, converting it into 2,5-bis-hydroxymethylfuran and 2,5-furandicarboxylic acid. Two enzymes groups, which belong to the ligninolytic system, aryl-alcohol oxidases and a dehydrogenase, are involved in this process. 5-Hydroxymethylfurfural induces the transcription and production of these enzymes, accompanied by an increase in activity levels
-
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
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
-
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). B4F334_CHRTR
623
0
69333
TrEMBL
other Location (Reliability: 2)
D3YBH4_PLEER
593
0
63621
TrEMBL
other Location (Reliability: 3)
E3Q9X3_COLGM
Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212)
711
0
76774
TrEMBL
-
E6PBN4_FUSO4
Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936)
679
0
73032
TrEMBL
-
E6PBP1_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
679
0
73014
TrEMBL
-
G2PZJ2_THET4
Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)
647
0
69130
TrEMBL
Mitochondrion (Reliability: 2)
I7FDJ2_ASPTE
666
0
74475
TrEMBL
other Location (Reliability: 4)
O94219_PLEER
593
0
63709
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61847
x * 61847, recombinant enzyme from Escherichia coli, mass spectrometry, x * 69114, wild-type enzyme, mass spectrometry, x * 69792, recombinant enzyme from Emericella nidulans, mass spectrometry
66700
67100
x * 67100, CtSAO without signal peptide, calculated from sequence
67700
69114
x * 61847, recombinant enzyme from Escherichia coli, mass spectrometry, x * 69114, wild-type enzyme, mass spectrometry, x * 69792, recombinant enzyme from Emericella nidulans, mass spectrometry
69792
x * 61847, recombinant enzyme from Escherichia coli, mass spectrometry, x * 69114, wild-type enzyme, mass spectrometry, x * 69792, recombinant enzyme from Emericella nidulans, mass spectrometry
70000
71000
80000
additional information
66700
x * 66700, CpSAP without signal peptide, calculated from sequence
additional information
apparent mass of about 80 kDa determined by SDS-PAGE, molecular mass of 67.7 kDa deduced from sequence
additional information
-
apparent mass of about 80 kDa determined by SDS-PAGE, molecular mass of 67.7 kDa deduced from sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 67100, CtSAO without signal peptide, calculated from sequence
?
x * 77500, SDS-PAGE, and x * 77507, calculated from sequence, deglycosylated protein
?
-
x * 77500, SDS-PAGE, and x * 77507, calculated from sequence, deglycosylated protein
-
?
x * 62600, calculated from sequence, x * 65600, SDS-PAGE of endoH-treated protein
?
x * 61847, recombinant enzyme from Escherichia coli, mass spectrometry, x * 69114, wild-type enzyme, mass spectrometry, x * 69792, recombinant enzyme from Emericella nidulans, mass spectrometry
?
-
x * 61485, recombinant enzyme mutant H91N, mass spectrometry, x * 61847, recombinant wild-type enzyme, mass spectrometry, x * 61088, recombinant wild-type enzyme, sequence calculation, x * recombinant enzyme mutant H91N, sequence calculation, x * 65000, recombinant wild-type enzyme, SDS-PAGE, x * 120000, recombinant enzyme mutant H91N, SDS-PAGE
?
x * 150000, recombinant protein from wild-type Saccharomyces cerevisiae, x * 63000, recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, x * 63000, recombinant protein from wild-type Pichia pastoris
monomer
structure-function relationship and analysis, structure comparison, overview
monomer
1 * 100000, recombinant protein, 1 * 70000, PNGase F-treated protein, SDS-PAGE, 1 * 60800, calculated from sequence
additional information
-
the molecular model of AAO from Pleurotus eryngii, PDB entry 1QJN, shows that it is a globular protein with common features with the overall structure topology of the other members of glucose-methanol-choline oxidoreductases family
additional information
-
N-terminal amino acid analysis, identical for isozymes i, II, III
additional information
the enzyme in SDS-PAGE gives several bands of 73, 65, 58, 47.5, and 20 kDa, peptide mapping, overview
additional information
-
the enzyme in SDS-PAGE gives several bands of 73, 65, 58, 47.5, and 20 kDa, peptide mapping, overview
additional information
-
the enzyme in SDS-PAGE gives several bands of 73, 65, 58, 47.5, and 20 kDa, peptide mapping, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
-
the enzyme contains no putative N/O-glycosylation sites
glycoprotein
presence of hybrid type structures (GlcNAc Man5-6 GlcNAc2)
glycoprotein
N-glycosylation predicted by data obtained from microsequencing
glycoprotein
N-glycosylation predicted by data obtained from microsequencing
glycoprotein
protein is predicted to be N-glycosylated on sites N309, N386, and N644
glycoprotein
-
protein is predicted to be N-glycosylated on sites N309, N386, and N644
-
glycoprotein
the amino acid sequence contains four and seven possible sites of N-glycosylation and O-glycosylation, respectively
glycoprotein
recombinant protein from wild-type Saccharomyces cerevisiae, 60% glycosylation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The central, seven-bladed beta-propeller domain and the C-terminal, immunoglobulin-like beta-sandwich together constitute the AA5_2 catalytic module (residues Val199 to Leu689). The N-terminal domain contains conserved disulfide bridges and an overall fold typical of a PAN_1 domain
sitting drop vapor diffusion method, using 1 M Li2SO4, 0.1 M bis-Tris propane pH 7.4
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y334F
mutant exhibits specific activities comparable to the wild-type for carbohydrates, diols, aryl alcohols, 5-hydroxymethylfurfural and 5-hydroxymethyl-2-furancarboxylic acid
Y334W
mutant exhibits increased specific activity toward carbohydrates and decreased activity toward diols, aryl alcohols, and furans
Y334F
-
mutant exhibits specific activities comparable to the wild-type for carbohydrates, diols, aryl alcohols, 5-hydroxymethylfurfural and 5-hydroxymethyl-2-furancarboxylic acid
-
Y334W
-
mutant exhibits increased specific activity toward carbohydrates and decreased activity toward diols, aryl alcohols, and furans
-
L416F
mutation decreases the activity with aromatic alcohols but maintains the activity with trans,trans-2,4-hexadien-1-ol
L416W
mutation decreases the activity with aromatic alcohols but maintains the activity with trans,trans-2,4-hexadien-1-ol
V465T
significant improvement of conversion rate and enantioselectivity with sec-allylic alcohols
A77W/R80C/H91N/L170M/V340A/I500M/F501W
best performer with substrate (S)-1-(4-methoxyphenyl)-ethanol, with a total 800fold enhancement of activity relative to the parental type
F397Y
mutant shows improved production of 2,5-furandicarboxylic acid, with 70% yield
F501A
F501H
mutant shows improved production of 2,5-furandicarboxylic acid, with 97% yield
F501W
site-directed mutagenesis, the mutant shows a twofold increase in O2 reactivity compared to the wild-type enzyme
F501Y
H502A
H502R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H502S
H546A
site-directed mutagenesis, the mutant shows over 35fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme
H546R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H546S
H91N
-
random mutageneis, the FX7 mutant (harboring the H91N mutation) shows a dramatic 96fold improvement in total activity with secretion levels of 2 mg/liter. Analysis of the N-terminal sequence of the FX7 variant confirms the correct processing of the prealphaproK hybrid peptide by the KEX2 protease. FX7 shows higher stability in terms of pH and temperature, whereas the pH activity profiles and the kinetic parameters are maintained. The Asn91 lies in the flavin attachment loop motif, and it is a highly conserved residue in all members of the GMC superfamily, except for Pleurotus eryngii and Pleurotus pulmonarius AAO. FX7 mutant homology modeling using the crystal structure of the AAO from Pleurotus eryngii at a resolution of 2.55 A, PDB ID 3FIM, structure-function analysis
H91N/L170M
H91N/L170M/F501W
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/I500L/F501I
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500L/F501I present a 15fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol
H91N/L170M/I500M/F501V
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500M/F501V present a 30fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol
H91N/L170M/I500M/F501W
H91N/L170M/I500Q/F501W
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500Q/F501W present a 5fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol
I500M
mutant shows improved production of 2,5-furandicarboxylic acid, with 80% yield
I500M/F501 W
mutant shows improved production of 2,5-furandicarboxylic acid, reaching a total turnover number over 16,000 in presence of 15 mM 5-hydroxymethylfurfural
L315A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y78A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
Y92F
Y92L
Y92W
additional information
F501A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F501A
-
site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview
F501A
the AAO preference for (S)-1-(4-fluorophenyl)ethanol is increased threefold when the bulky side chain of Phe501 is removed in the F501A variant, which shows a stereoselectivity S/R ratio of 66:1 for this secondary alcohol
F501A
site-directed mutagenesis, the mutant shows strongly reduced O2 reactivity compared to the wild-type enzyme
F501Y
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F501Y
-
site-directed mutagenesis, kinetics and redox potential compared to the wild-type enzyme, overview
H502A
site-directed mutagenesis, the mutant shows over 1800fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity, compared to the wild-type enzyme
H502A
site-directed mutagenesis, the mutant shows 3000fold and 1800fold decreased kcat and kred compared to the wild-type enzyme
H502A
site-directed mutagenesis, the mutant shows over 1800fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity, compared to the wild-type enzyme
H502S
the mutant shows much lower activities on 4-nitrobenzaldehyde (340fold activity decrease) than the wild type enzyme
H502S
site-directed mutagenesis, the mutant shows over 1200fold decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme
H546S
the mutant shows much lower activities on 4-nitrobenzaldehyde (670fold activity decrease) than the wild type enzyme
H546S
site-directed mutagenesis, the mutant shows decreased both catalytic and transient-state reduction constants for 4-methoxybenzyl alcohol, as well as a strong decrease in the alcohol affinity compared to the wild-type enzyme
H91N/L170M
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M
expression variant carrying 4 mutations in the chimeric signal peptide (prealphaproK), plus mutations H91N/L170M in the mature protein, shows increased secretion upon expression in Pichia pastoris and Saccharomyces cerevisiae
H91N/L170M/I500M/F501W
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
H91N/L170M/I500M/F501W
mutation H91N in an alpha-helix situated at the protein surface, and the consensus mutation H91N in the FAD attachment loop, to enhance stability and improve production by Saccharomyces cerevisiae to 4.5 mg/l and by Pichia pastoris in a bioreactor to 25.5 mg/l. I500M/F501W present a 160fold enhancement in activity with substrate (S)-1-(4-methoxyphenyl)-ethanol, while the specific activity on primary alcohols is dramatically reduced
Y92F
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
Y92F
the mutation causes a 5fold reduction in the p-anisaldehyde kcat value
Y92F
site-directed mutagenesis, replacement of Tyr92 by phenylalanine does not alter the AAO kinetic constants (on 4-methoxybenzyl alcohol), compared to the wild-type enzyme, most probably because the stacking interaction is still possible
Y92F
mutation of active site, residue is involved in modulating the hydride transfer reaction
Y92L
site-directed mutagenesis, replacement with a leucine produces a decrease in catalytic efficiency for the alcohol substrate (2.6fold lower), accompanied by approximately twofold increases in both Km(Al) and Kd compared to the wild-type enzyme. The mutation causes a strong decrease in catalytic efficiencies for both O2 (6fold lower) and 4-methoxybenzyl alcohol (860fold lower). As the turnover rate for the Y92W variant is reduced tenfold, the main effect of the mutation concerns the availability of the alcohol substrate at the AAO active site (with 75fold higher Km values). The stacking interactions are strongly affected by this mutation
Y92L
mutation of active site, residue is involved in modulating the hydride transfer reaction
Y92W
site-directed mutagenesis, introduction of a tryptophan residue at this position only causes a slight increase in KMO2, but strongly reduces the affinity for the substrate (i.e. the pre-steady state Kd and steady-state Km increase by 150fold and 75fold, respectively) and therefore the steady-state catalytic efficiency, compared to the wild-type enzyme, suggesting that proper stacking is impossible with this bulky residue
Y92W
mutation of active site, residue is involved in modulating the hydride transfer reaction
additional information
-
wild-type and mutant enzymes are adsorbed on graphite electrodes or with the enzymes in solution using glassy carbon electrode as working electrode, activity analysis, overview
additional information
-
in vitro involution of the enzyme by restoring the consensus ancestor Asn91 promotes AAO expression and stability. The native signal sequence of AAO from Pleurotus eryngii is replaced by those of the mating alpha-factor and the K1 killer toxin, as well as different chimeras of both prepro-leaders in order to drive secretion in Saccharomyces cerevisiae strain BJ5465. The secretion of these mutant AAO constructs increase in the following descending order: preproalpha-AAO, prealphaproK-AAO, preKproalpha-AAO, preproK-AAO. The chimeric prealphaproK-AAO is subjected to focused-directed evolution with the aid of a dual screening assay based on the Fenton reaction. Random mutagenesis and DNA recombination is concentrated on two protein segments (Met[alpha1]-Val109 and Phe392-Gln566), and an array of improved variants is identified
additional information
a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5
additional information
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5
additional information
-
a two-enzyme system comprising a dye decolorizing peroxidase (DyP) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
6 - 9
the recombinant enzyme demonstrates partial pH stability in range from pH 6.0 to pH 9.0 after 1 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
initial loss of 10% of activity, thereafter stable or at least 22 h
30 - 70
the enzyme is stable up to 30°C and the stability is greatly reduced at 40°C (50% inactivation) and leads to 100% inactivation after 5 min at 70°C
35
37 - 50
the enzyme loses 86% of its activity after 12 min at 50°C, while it remains stable at 37°C for more than 20 min and retains about 90% of its activity after 1 h
50
55
60
61.2
melting temperature, recombinant protein from glycosylation-deficient Saccharomyces cerevisiae
61.3
melting temperature, recombinant protein from wild-type Pichia pastoris
63
melting temperature, recombinant protein from wild-type Saccharomyces cerevisiae
60
half-life 10 min in absence of Ca2+, in presence of Ca2+ activity is maintained for 2 h
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexafluorobenzene
improved conversion of up to 99% in 50-90% , v/v
additional information
additional information
the enantioselectivity of the reaction with sec-allylic alcohols can be tuned by applying either pressure or by the addition of cosolvents sucgh as DMSO, isooctane, glycerol, n-heptane, methynol, ethanol, acetone, DMF
additional information
the enzyme activity decreases at elevated concentrations of water-miscible polar solvents, while the presence of (halogenated) hydrocarbons is tolerated up to 90% (v/v)
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration
native enzyme 24.4fold to homogeneity by anion exchange chromatography and gel filtration
-
recombinant enzyme from Emericella nidulans by gel filtration and anion exchange chromatography
-
recombinant enzyme, expressed and secreted from Coprinopsis cinerea strain FA2222, 72fold from culture supernatant by cross-flow filtration, anion exchange chromatography, and two different steps of gel filtration
recombinant FLAG1-tagged enzyme in Escherichia coli strain W3110 solubilized from inclusion bodies 9.6fold by anion exchange chromatography
recombinant mature enzyme from Escherichia coli by anion exchange chromatography
recombinant protein
recombinant wild-type and mutant emzymes from Escherichia coli to homogeneity
three-phase partitioning with 30% (w/v) of ammonium sulfate and t-butanol (1:1 ratio)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, recombinant expression in Escherichia coli
expression in Aspergillus nidulans, activity of the recombinant enzyme in Aspergillus nidulans culture is much higher than in extracellular fluid of Pleurotus eryngii
-
expression in Emericella nidulans under control of the fungal alc promoter
-
expression in Escherichia coli
expression in Pichia pastoris
expression of the constructs encoding CpSAO in Escherichia coli BL21(DE3) results in the formation of insoluble inclusion bodies. The expression construct is coexpressed with the plasmid pREP4-groESL, encoding chaperonine proteins of the Hsp60 family (GroEL and GroES). Coexpression at 15°C for 16 h results in the formation of soluble recombinant SAO
expression of the constructs encoding CtSAO in Escherichia coli BL21(DE3) results in the formation of insoluble inclusion bodies. The expression construct is coexpressed with the plasmid pREP4-groESL, encoding chaperonine proteins of the Hsp60 family (GroEL and GroES). Coexpression at 15°C for 16 h results in the formation of soluble recombinant SAO
expression of wild-type and mutant enzymes in Emericella nidulans under control of the inducible fungal alc promoter
-
expression of wild-type enzyme in Escherichia coli, expression of wild-type and mutant enzymes in Emericella nidulans
-
gene aao, expression of FLAG1-tagged enzyme in Escherichia coli strain W3110, the non-glycosylated recombinant enzyme is successfully activated in vitro after Escherichia coli expression in form of inclusion bodies, expression iand glycosylation of the enzyme in Emericella nidulans strain IJFM A729
gene aao, expression of wild-type and mutant emzymes in Escherichia coli
gene aao, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
gene aao, subcloning in Saccharomyces cerevisiae strain RH1385 for the plasmid construction via homologous recombination, heterologous recombinant expression in Coprinopsis cinerea strain FA2222 under control of the promotor of the glyceraldehyde-3-phosphate dehydrogenase gene 2 (gpdII) of the button mushroom Agaricus bisporus, and enzyme secretion to the culture medium. It might be that Coprinopsis cinerea does not provide the needed signal peptidase required for cleavage of the Pleurotus sapidus AAO signal peptide
gene gloA, recombinant expression in Aspergillus nidulans strain 773, method optimization using agitated and static cultures with or without pyridoxine, pyridoxine has a positive effect on enzyme production
-
in fusion with chimeric prepro-leader (pre-alpha-factor-proKiller) that enhances secretion by introducing the F[3alpha]S, N[25proK]D, T[50proK]A and F[52proK]L mutations
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
compared with the control, inducers increased the AAO production in Pleurotus ostreatus in the following order: L-tyrosine (5 mM) > veratryl alcohol (7 mM) > benzyl alcohol (10 mM) > L-phenylalanine (5 mM) > 4-anisyl alcohol (9 mM)
-
expression is induced in presence of 5-hydroxymethylfurfural
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the non-glycosylated recombinant enzyme is successfully activated in vitro after Escherichia coli expression in form of inclusion bodies
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
-
the enzyme in white-rot fungi is useful in degradation of aromatic hydrocarbons in a historically contaminated soil
synthesis
additional information
synthesis
due to hydride-transfer stereoselectivity and specificity on substituted aldehydes, the enzyme is useful for flavor production and in production of chiral compounds. Flavor synthesis and enzyme stereoselectivity, overview
synthesis
AAO is able to produce 2,5-furandicarboxylic acid from formylfurancarboxylic acid, allowing full oxidation of 5-hydroxymethylfurfural. During 5-hydroxymethylfurfural reactions, an inhibitory effect of the H2O2 produced in the first two oxidation steps is the cause of the lack of AAO activity on formylfurancarboxylic acid. 5-Hydroxymethylfurfural is successfully converted into 2,5-furandicarboxylic acid when the AAO reaction is carried out in the presence of catalase
synthesis
high-yield production of AAO in submerged culture using a recombinant Aspergillus nidulans strain grown on corn steep liquor. The optimum medium component concentrations are 61.0 g/l maltose, 26.4 g/L corn steep liquor, and 13.8 g/l NaNO3. The greatest AAO activity achieved is 1021 U/l with a protein concentration of 0.75 g/l
synthesis
production of AAO using Aspergillus nidulans in a stirred-tank bioreactor. pH control significantly affects protein production and increasing dissolved oxygen level stimulates AAO production. The greatest AAO activity (1906 U/l) and protein concentration (1.19 g/l) are achieved in 48 h at 60% dissolved oxygen with pH controlled at 6.0. The yield and productivity (in 48 h) are 31.2 U/g maltose and 39.7 U/l/h, respectively
synthesis
expression and secretion of AAO with yield of 315 mg/l using Pichia pastoris
synthesis
Mn(OAc)3 functions as a suitable activator for several commercially available variants of GOase with a series of alcohol substrates. Use of the Mn(OAc)3 additive is also compatible with biocatalytic synthesis of islatravir and subsequent biocatalytic steps in the islatravir-forming cascade
synthesis
enantioselective oxidation of sec-allylic alcohols using variants of the berberine bridge enzyme analogue from Arabidopsis thaliana (AtBBE15) and the 5-(hydroxymethyl)furfural oxidase (HMFO) and its variants V465T, V465S, V465T/W466H and V367R/W466F. The enantioselectivity can be tuned by applying either pressure or by the addition of cosolvents
synthesis
-
construction of fusion proteins with Saccharomyces cerevisiae unspecific peroxidase, EC 1.11.2.1, using different peptide linkers. The reaction system is optimized to control the aromatic alcohol transformation rate, and therefore the H2O2 supply, to achieve total turnover numbers of 62000 for the biocatalytic synthesis of dextrorphan, a metabolite of the antitussive drug dextromethorphan
synthesis
biooxidation of benzylic alcohols in the presence of various organic (co)solvents. The enzyme activity decreases at elevated concentrations of water-miscible polar solvents, while the presence of (halogenated) hydrocarbons is tolerated up to 90% (v/v), which leads to drastically improved conversions of up to >99% in case of hexafluorobenzene. This effect is correlated with the improved solubility of O2 in the employed solvents
synthesis
selective oxidation of (2E)-hex-2-en-1-ol to the corresponding aldehyde using recombinant aryl alcohol oxidase. The application of a two liquid phase system to overcome solubility and product inhibition issues yields more than 2200000 catalytic turnovers for the enzyme as well as molar product concentrations
synthesis
expression variant carrying 4 mutations in the chimeric signal peptide (prealphaproK), plus mutations H91N/L170M in the mature protein, shows 350fold improved secretion (4.5 mg/l) in Saccharomyces cerevisiae and is stable. Expression in Pichia pastoris and fermentation in a fed-batch bioreactor enhances production to 25 mg/l. Both recombinant AAO from Saccharomyces cerevisiae and Pichia pastoris are subjected to the same N-terminal processing and have a similar pH activity profile, they differ in their kinetic parameters and thermostability
synthesis
Thermothelomyces thermophilus DSM 1799
-
high-yield production of AAO in submerged culture using a recombinant Aspergillus nidulans strain grown on corn steep liquor. The optimum medium component concentrations are 61.0 g/l maltose, 26.4 g/L corn steep liquor, and 13.8 g/l NaNO3. The greatest AAO activity achieved is 1021 U/l with a protein concentration of 0.75 g/l
-
synthesis
Thermothelomyces thermophilus DSM 1799
-
production of AAO using Aspergillus nidulans in a stirred-tank bioreactor. pH control significantly affects protein production and increasing dissolved oxygen level stimulates AAO production. The greatest AAO activity (1906 U/l) and protein concentration (1.19 g/l) are achieved in 48 h at 60% dissolved oxygen with pH controlled at 6.0. The yield and productivity (in 48 h) are 31.2 U/g maltose and 39.7 U/l/h, respectively
-
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
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
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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Muheim, A.; Leisola, M.S.A.; Schoemaker, H.E.
Aryl-alcohol oxidase and lignin peroxidase from the white-rot fungus Bjerkandera adusta
J. Biotechnol.
13
159-167
1990
no activity in Phanerochaete chrysosporium, Bjerkandera adusta
-
brenda
Guillen, F.; Martinez, A.T.; Martinez, M.J.
Production of hydrogen peroxide by aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryhgii
Appl. Microbiol. Biotechnol.
32
465-469
1990
Pleurotus eryngii
-
brenda
Muheim, A.; Waldner, R.; Leisola, M.S.A.; Fiechter, A.
An extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta
Enzyme Microb. Technol.
12
204-209
1990
Bjerkandera adusta
-
brenda
Waldner, R.; Leisola, M.S.A.; Fiechter, A.
Comparison of ligninolytic activities of selected white-rot fungi
Appl. Microbiol. Biotechnol.
29
400-407
1988
Bjerkandera adusta, Phanerodontia chrysosporium, Trametes versicolor, Rigidoporus microporus, Pleurotus ostreatus
-
brenda
Bourbonnais, R.; Paice, M.G.
Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju
Biochem. J.
255
445-450
1988
Lentinus sajor-caju
brenda
Farmer, V.C.; Henderson, M.E.K.; Russell, J.D.
Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor
Biochem. J.
74
257-262
1960
Trametes versicolor
brenda
Mann, V.; Large, A.; Khan, S.; Malik, Z.; Connock, M.J.
Aromatic alcohol oxidase: a new membrane-bound H2O2-generating enzyme in alimentary tiddues of the slug Arion ater
J. Exp. Zool.
251
265-274
1989
Arion ater
-
brenda
Marzullo, L.; Cannio, R.; Giardina, P.; Santini, M.T.; Sannia, G.
Veratryl alcohol oxidase from Pleurotus ostreatus participates in lignin biodegradation and prevents polymerization of laccase-oxidized substrates
J. Biol. Chem.
270
3823-3827
1995
Pleurotus ostreatus
brenda
Varela, E.; Martinez, A.T.; Martinez, M.J.
Molecular cloning of aryl-alcohol oxidase from the fungus Pleurotus eryngii, an enzyme involved in lignin degradation
Biochem. J.
341
113-117
1999
Pleurotus eryngii
-
brenda
Varela, E.; Guillen, F.; Martinez, A.T.; Martinez, M.J.
Expression of Pleurotus eryngii aryl-alcohol oxidase in Aspergillus nidulans: purification and characterization of the recombinant enzyme
Biochim. Biophys. Acta
1546
107-113
2001
Pleurotus eryngii
brenda
Varela, E.; Bockle, B.; Romero, A.; Martinez, A.T.; Martinez, M.J.
Biochemical characterization, cDNA cloning and protein crystallization of aryl-alcohol oxidase from Pleurotus pulmonarius
Biochim. Biophys. Acta
1476
129-138
2000
Pleurotus pulmonarius
brenda
Asada, Y.; Watanabe, A.; Ohtsu, Y.; Kuwahara, M.
Purification and characterization of an aryl-alcohol oxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium
Biosci. Biotechnol. Biochem.
59
1339-1341
1995
Phanerodontia chrysosporium
-
brenda
Guillen, F.; Martinez, A.T.; Martinez, M.J.
Substrate specificity and properties of the aryl-alcohol oxidase from ligninolytic fungus Pleurotus eryngii
Eur. J. Biochem.
209
603-611
1992
Pleurotus eryngii
brenda
Brckmann, M.; Termonia, A.; Pasteels, J.M.; Hartmann, T.
Characterization of an extracellular salicyl alcohol oxidase from larval defensive secretions of Chrysomela populi and Phratora vitellinae (Chrysomelina)
Insect Biochem. Mol. Biol.
32
1517-1523
2002
Chrysomela populi, Phratora vitellinae
brenda
Okamoto, K.; Yanase, H.
Aryl alcohol oxidases from the white-rot basidiomycete Pleurotus ostreatus
Mycoscience
43
391-395
2002
Pleurotus ostreatus
-
brenda
Kumar, A.K.; Goswami, P.
Functional characterization of alcohol oxidases from Aspergillus terreus MTCC 6324
Appl. Microbiol. Biotechnol.
72
906-911
2006
Aspergillus terreus, Aspergillus terreus MTCC 6324
brenda
Ferreira, P.; Medina, M.; Guillen, F.; Martinez, M.J.; Van Berkel, W.J.; Martinez, A.T.
Spectral and catalytic properties of aryl-alcohol oxidase, a fungal flavoenzyme acting on polyunsaturated alcohols
Biochem. J.
389
731-738
2005
Pleurotus eryngii
brenda
Sampedro, I.; DAnnibale, A.; Ocampo, J.A.; Stazi, S.R.; Garcia-Romera, I.
Solid-state cultures of Fusarium oxysporum transform aromatic components of olive-mill dry residue and reduce its phytotoxicity
Biores. Technol.
98
3547-3554
2007
no activity in Fusarium oxysporum, no activity in Fusarium oxysporum BAFC 738
brenda
D'Annibale, A.; Ricci, M.; Leonardi, V.; Quaratino, D.; Mincione, E.; Petruccioli, M.
Degradation of aromatic hydrocarbons by white-rot fungi in a historically contaminated soil
Biotechnol. Bioeng.
90
723-731
2005
Pleurotus pulmonarius, no activity in Phanerochaete chrysosporium, no activity in Phanerochaete chrysosporium NRRL 6361
brenda
Kabe, Y.; Osawa, T.; Ishihara, A.; Kabe, T.
Decolorization of coal humic acid by extracellular enzymes produced by white-rot fungi
Coal Prep.
25
211-220
2005
Pleurotus pulmonarius
-
brenda
Ferreira, P.; Ruiz-Duenas, F.J.; Martinez, M.J.; van Berkel, W.J.; Martinez, A.T.
Site-directed mutagenesis of selected residues at the active site of aryl-alcohol oxidase, an H2O2-producing ligninolytic enzyme
FEBS J.
273
4878-4888
2006
Pleurotus eryngii
brenda
Saparrata, M.C.; Guillen, F.
Ligninolytic ability and potential biotechnology applications of the south american fungus Pleurotus laciniatocrenatus
Folia Microbiol. (Praha)
50
155-160
2005
Pleurotus laciniatocrenatus
brenda
Madhurendr, M.; Prasad, N.
Veratryl alcohol oxidase and laccase activity in Pleurotus spp
J. Plant Biol.
32
129-132
2005
Pleurotus ostreatus, Lentinus sajor-caju
-
brenda
Ruiz-Duenas, F.J.; Ferreira, P.; Martinez, M.J.; Martinez, A.T.
In vitro activation, purification, and characterization of Escherichia coli expressed aryl-alcohol oxidase, a unique H2O2-producing enzyme
Protein Expr. Purif.
45
191-199
2006
Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Michalski, C.; Mohagheghi, H.; Nimtz, M.; Pasteels, J.; Ober, D.
Salicyl alcohol oxidase of the chemical defense secretion of two chrysomelid leaf beetles: Molecular and functional characterization of two new members of the GMC oxidoreductase gene family
J. Biol. Chem.
283
19219-19228
2008
Chrysomela populi (B4F335), Chrysomela populi, Chrysomela tremula (B4F334), Chrysomela tremula
brenda
Ferreira, P.; Hernandez-Ortega, A.; Herguedas, B.; Martinez, A.T.; Medina, M.
Aryl-alcohol oxidase involved in lignin degradation: a mechanistic study based on steady and pre-steady state kinetics and primary and solvent isotope effects with two alcohol substrates
J. Biol. Chem.
284
24840-24847
2009
Pleurotus eryngii (O94219)
brenda
Munteanu, F.; Ferreira, P.; Ruiz-Duenas, F.; Martinez, A.; Cavaco-Paulo, A.
ioelectrochemical investigations of aryl-alcohol oxidase from Pleurotus eryngii
J. Electroanal. Chem.
618
83-86
2008
Pleurotus eryngii
-
brenda
Fernandez, I.S.; Ruiz-Duenas, F.J.; Santillana, E.; Ferreira, P.; Martinez, M.J.; Martinez, A.T.; Romero, A.
Novel structural features in the GMC family of oxidoreductases revealed by the crystal structure of fungal aryl-alcohol oxidase
Acta Crystallogr. Sect. D
65
1196-1205
2009
Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Kumar, V.V.; Rapheal, V.S.
Induction and purification by three-phase partitioning of aryl alcohol oxidase (AAO) from Pleurotus ostreatus
Appl. Biochem. Biotechnol.
163
423-432
2011
Pleurotus ostreatus
brenda
Ferreira, P.; Hernandez-Ortega, A.; Herguedas, B.; Rencoret, J.; Gutierrez, A.; Martinez, M.J.; Jimenez-Barbero, J.; Medina, M.; Martinez, A.T.
Kinetic and chemical characterization of aldehyde oxidation by fungal aryl-alcohol oxidase
Biochem. J.
425
585-593
2010
Pleurotus eryngii (O94219)
brenda
Lupo, S.; Perez, A.; Martinez, S.; Simeto, S.; Rivas, F.; Bettucci, L.
In vitro characterization of Inocutis jamaicensis and experimental inoculation of Eucalyptus globulus standing trees
Forest Pathol.
39
293-303
2009
no activity in Inocutis jamaicensis
-
brenda
Hernandez-Ortega, A.; Ferreira, P.; Martinez, A.T.
Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation
Appl. Microbiol. Biotechnol.
93
1395-1410
2012
Pleurotus eryngii (O94219), Pleurotus eryngii, Rhodonia placenta, Phanerodontia chrysosporium, Trametes versicolor, Fusarium solani, Rigidoporus microporus, Bjerkandera adusta, Botrytis cinerea
brenda
Hernandez-Ortega, A.; Borrelli, K.; Ferreira, P.; Medina, M.; Martinez, A.T.; Guallar, V.
Substrate diffusion and oxidation in GMC oxidoreductases: an experimental and computational study on fungal aryl-alcohol oxidase
Biochem. J.
436
341-350
2011
Pleurotus eryngii (O94219)
brenda
Hernandez-Ortega, A.; Lucas, F.; Ferreira, P.; Medina, M.; Guallar, V.; Martinez, A.T.
Role of active site histidines in the two half-reactions of the aryl-alcohol oxidase catalytic cycle
Biochemistry
51
6595-6608
2012
Pleurotus eryngii (O94219)
brenda
Tamboli, D.; Telke, A.; Dawkar, V.; Jadhav, S.; Govindwar, S.
Purification and characterization of bacterial aryl alcohol oxidase from Sphingobacterium sp. ATM and its uses in textile dye decolorization
Biotechnol. Bioprocess Eng.
16
661-668
2011
Sphingobacterium sp., Sphingobacterium sp. ATM
-
brenda
Hernandez-Ortega, A.; Ferreira, P.; Merino, P.; Medina, M.; Guallar, V.; Martinez, A.T.
Stereoselective hydride transfer by aryl-alcohol oxidase, a member of the GMC superfamily
ChemBioChem
13
427-435
2012
Pleurotus eryngii (O94219)
brenda
Hernandez-Ortega, A.; Lucas, F.; Ferreira, P.; Medina, M.; Guallar, V.; Martinez, A.T.
Modulating O2 reactivity in a fungal flavoenzyme: involvement of aryl-alcohol oxidase Phe-501 contiguous to catalytic histidine
J. Biol. Chem.
286
41105-41114
2011
Pleurotus eryngii (O94219)
brenda
Chakraborty, M.; Goel, M.; Chinnadayyala, S.R.; Dahiya, U.R.; Ghosh, S.S.; Goswami, P.
Molecular characterization and expression of a novel alcohol oxidase from Aspergillus terreus MTCC6324
PLoS ONE
9
e95368
2014
Aspergillus terreus (I7FDJ2), Aspergillus terreus MTCC6324 (I7FDJ2)
brenda
Vina-Gonzalez, J.; Gonzalez-Perez, D.; Ferreira, P.; Martinez, A.T.; Alcalde, M.
Focused directed evolution of aryl-alcohol oxidase in Saccharomyces cerevisiae by using chimeric signal peptides
Appl. Environ. Microbiol.
81
6451-6462
2015
Pleurotus eryngii
brenda
Couturier, M.; Mathieu, Y.; Li, A.; Navarro, D.; Drula, E.; Haon, M.; Grisel, S.; Ludwig, R.; Berrin, J.G.
Characterization of a new aryl-alcohol oxidase secreted by the phytopathogenic fungus Ustilago maydis
Appl. Microbiol. Biotechnol.
100
697-706
2016
Mycosarcoma maydis
brenda
Galperin, I.; Javeed, A.; Luig, H.; Lochnit, G.; Ruehl, M.
An aryl-alcohol oxidase of Pleurotus sapidus heterologous expression, characterization, and application in a 2-enzyme system
Appl. Microbiol. Biotechnol.
100
8021-8030
2016
Pleurotus sapidus (A0A145Y386), Pleurotus sapidus, Pleurotus sapidus DSM 8266 (A0A145Y386)
brenda
Feldman, D.; Kowbel, D.J.; Glass, N.L.; Yarden, O.; Hadar, Y.
Detoxification of 5-hydroxymethylfurfural by the Pleurotus ostreatus lignolytic enzymes aryl alcohol oxidase and dehydrogenase
Biotechnol. Biofuels
8
63
2015
Pleurotus ostreatus (E5CZV8), Pleurotus ostreatus
brenda
Ferreira, P.; Hernandez-Ortega, A.; Lucas, F.; Carro, J.; Herguedas, B.; Borrelli, K.W.; Guallar, V.; Martinez, A.T.; Medina, M.
Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
FEBS J.
282
3091-3106
2015
Pleurotus eryngii (O94219)
brenda
Pardo-Planas, O.; Prade, R.A.; Wilkins, M.R.
High-yield production of aryl alcohol oxidase under limited growth conditions in small-scale systems using a mutant Aspergillus nidulans strain
J. Ind. Microbiol. Biotechnol.
44
247-257
2017
Thermothelomyces thermophilus
brenda
Gomez De Santos, P.; Lazaro, S.; Vin-Gonzalez, J.; Hoang, M.; Sanchez-Moreno, I.; Glieder, A.; Hollmann, F.; Alcalde, M.
Evolved peroxygenase-aryl alcohol oxidase fusions for self-sufficient oxyfunctionalization reactions
ACS Catal.
10
13524-13534
2020
Komagataella pastoris
-
brenda
Mathieu, Y.; Offen, W.; Forget, S.; Ciano, L.; Viborg, A.; Blagova, E.; Henrissat, B.; Walton, P.; Davies, G.; Brumer, H.
Discovery of a fungal copper radical oxidase with high catalytic efficiency toward 5-hydroxymethylfurfural and benzyl alcohols for bioprocessing
ACS Catal.
10
3042-3058
2020
Colletotrichum graminicola (E3Q9X3), Colletotrichum graminicola M1.001 (E3Q9X3)
-
brenda
Vina-Gonzalez, J.; Jimenez-Lalana, D.; Sancho, F.; Serrano, A.; Martinez, A.; Guallar, V.; Alcalde, M.
Structure-guided evolution of aryl alcohol oxidase from Pleurotus eryngii for the selective oxidation of secondary benzyl alcohols
Adv. Synth. Catal.
361
2514-2525
2019
Pleurotus eryngii (O94219)
-
brenda
de Almeida, T.; van Schie, M.; Ma, A.; Tieves, F.; Younes, S.; Fernandez-Fueyo, E.; Arends, I.; Riul, A.J.; Hollmann, F.
Efficient aerobic oxidation of trans-2-hexen-1-ol using the aryl alcohol oxidase from Pleurotus eryngii
Adv. Synth. Catal.
361
2668-2672
2019
Pleurotus eryngii (O94219)
-
brenda
Gandomkar, S.; Jost, E.; Loidolt, D.; Swoboda, A.; Pickl, M.; Elaily, W.; Daniel, B.; Fraaije, M.; Macheroux, P.; Kroutil, W.
Biocatalytic enantioselective oxidation of sec-allylic alcohols with flavin-dependent oxidases
Adv. Synth. Catal.
361
5264-5271
2019
Methylovorus sp. MP688 (E4QP00)
brenda
Vinambres, M.; Espada, M.; Martinez, A.T.; Serrano, A.
Screening and evaluation of new hydroxymethylfurfural oxidases for furandicarboxylic acid production
Appl. Environ. Microbiol.
86
e00842
2020
Methylovorus sp. MP688 (E4QP00), Pseudomonas nitroreducens, Pseudomonas sp. 11/12A
brenda
Jankowski, N.; Koschorreck, K.; Urlacher, V.B.
High-level expression of aryl-alcohol oxidase 2 from Pleurotus eryngii in Pichia pastoris for production of fragrances and bioactive precursors
Appl. Microbiol. Biotechnol.
104
9205-9218
2020
Pleurotus eryngii (D3YBH4), Pleurotus eryngii
brenda
Kadowaki, M.; Higasi, P.; de Godoy, M.; de Araujo, E.; Godoy, A.; Prade, R.; Polikarpov, I.
Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77
Biochim. Biophys. Acta
1864
129681
2020
Thermothelomyces thermophilus (G2PZJ2), Thermothelomyces thermophilus, Thermothelomyces thermophilus DSM 1799 (G2PZJ2)
brenda
Vina-Gonzalez, J.; Martinez, A.T.; Guallar, V.; Alcalde, M.
Sequential oxidation of 5-hydroxymethylfurfural to furan-2,5-dicarboxylic acid by an evolved aryl-alcohol oxidase
Biochim. Biophys. Acta
1868
140293
2020
Pleurotus eryngii (O94219)
brenda
Liu, E.; Li, M.; Abdella, A.; Wilkins, M.
Development of a cost-effective medium for submerged production of fungal aryl alcohol oxidase using a genetically modified Aspergillus nidulans strain
Biores. Technol.
305
123038
2020
Thermothelomyces thermophilus (G2PZJ2), Thermothelomyces thermophilus DSM 1799 (G2PZJ2)
brenda
Liu, E.; Wilkins, M.
Process optimization and scale-up production of fungal aryl alcohol oxidase from genetically modified Aspergillus nidulans in stirred-tank bioreactor
Biores. Technol.
315
123792
2020
Thermothelomyces thermophilus (G2PZJ2), Thermothelomyces thermophilus DSM 1799 (G2PZJ2)
brenda
Vina-Gonzalez, J.; Elbl, K.; Ponte, X.; Valero, F.; Alcalde, M.
Functional expression of aryl-alcohol oxidase in Saccharomyces cerevisiae and Pichia pastoris by directed evolution
Biotechnol. Bioeng.
115
1666-1674
2018
Pleurotus eryngii (O94219)
brenda
Serrano, A.; Calvino, E.; Carro, J.; Sanchez-Ruiz, M.I.; Canada, F.J.; Martinez, A.T.
Complete oxidation of hydroxymethylfurfural to furandicarboxylic acid by aryl-alcohol oxidase
Biotechnol. Biofuels
12
217
2019
Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Cleveland, M.; Lafond, M.; Xia, F.; Chung, R.; Mulyk, P.; Hein, J.; Brumer, H.
Two Fusarium copper radical oxidases with high activity on aryl alcohols
Biotechnol. Biofuels
14
138
2021
Fusarium graminearum (E6PBP1), Fusarium oxysporum f. sp. lycopersici (E6PBN4), Fusarium oxysporum f. sp. lycopersici 4287 (E6PBN4), Fusarium graminearum ATCC MYA-4620 (E6PBP1)
brenda
Tamaru, Y.; Umezawa, K.; Yoshida, M.
Characterization of an aryl-alcohol oxidase from the plant saprophytic basidiomycete Coprinopsis cinerea with broad substrate specificity against aromatic alcohols
Biotechnol. Lett.
40
1077-1086
2018
Coprinopsis cinerea (A0A2Z5WP81), Coprinopsis cinerea
brenda
Johnson, H.C.; Zhang, S.; Fryszkowska, A.; Ruccolo, S.; Robaire, S.A.; Klapars, A.; Patel, N.R.; Whittaker, A.M.; Huffman, M.A.; Strotman, N.A.
Biocatalytic oxidation of alcohols using galactose oxidase and a manganese(III) activator for the synthesis of islatravir
Org. Biomol. Chem.
19
1620-1625
2021
Fusarium graminearum (P0CS93)
brenda
Carro, J.; Martinez-Julvez, M.; Medina, M.; Martinez, A.T.; Ferreira, P.
Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase
Phys. Chem. Chem. Phys.
19
28666-28675
2017
Pleurotus eryngii (O94219), Pleurotus eryngii
brenda
Pickl, M.; Jost, E.; Glueck, S.; Faber, K.
Improved biooxidation of Benzyl alcohols catalyzed by the flavoprotein (5-hydroxymethyl)furfural oxidase in organic solvents
Tetrahedron
73
5408-5410
2017
Methylovorus sp. MP688 (E4QP00)
-
brenda
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