Any feedback?
Information on EC 1.1.3.7 - aryl-alcohol oxidase and Organism(s) Pleurotus eryngii and UniProt Accession O94219
for references in articles please use BRENDA:EC1.1.3.7Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.3.7 aryl-alcohol oxidaseIUBMB Comments
Oxidizes many primary alcohols containing an aromatic ring; best substrates are (2-naphthyl)methanol and 3-methoxybenzyl alcohol.
Specify your search results
Word Map
- 1.1.3.7
-
anodic
-
aluminum
-
fabric
-
nanoporous
-
porous
-
film
-
nanostructures
-
ascending
-
aorta
- lignin
-
nanowires
-
nanotube
- laccase
-
etch
-
nanochannels
-
ophthalmology
-
age-at-onset
-
academy
-
decolor
-
nanorods
- pleurotus
-
ligninolytic
-
white-rot
-
bicuspid
-
free-standing
- eryngii
-
electrodeposition
-
sputter
-
valsalva
-
large-area
-
template-assisted
- environmental protection
- synthesis
-
aortopathy
- bjerkandera
-
nanopillars
-
four-dimensional
-
nanopatterns
-
photovoltaic
-
polycrystalline
-
remazol
-
glucose-methanol-choline
-
president
-
nanoarrays
The taxonomic range for the selected organisms is: Pleurotus eryngii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aao, aryl-alcohol oxidase, veratryl alcohol oxidase, aryl alcohol oxidase, salicyl alcohol oxidase, arylalcohol oxidase, mtgloa, cpsao, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAO
-
AAO
arom. alcohol oxidase
-
-
-
-
aryl alcohol oxidase
-
-
-
-
oxidase, aryl alcohol
-
-
-
-
VAO
-
-
-
-
veratryl alcohol oxidase
-
-
-
-
additional information
AAO
-
-
-
-
additional information
the enzyme belongs to the the glucose-methanol-choline oxidase, GMC, family of oxidoreductases
additional information
-
the enzyme belongs to the glucose-methanol-choline oxidoreductases, GMC, family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
a sequential mechanism in which O2 reacts with reduced enzyme before release of the aldehyde product, the AAO reductive half-reaction is essentially irreversible and rate limiting during catalysis, a synchronous mechanism in which hydride transfer from substrate alpha-carbon to FAD and proton abstraction from hydroxyl occur simultaneously, reaction mechanism, overview. The AAO catalytic mechanism proceeds via electrophilic attack and direct transfer of a hydride to the flavin
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
catalytic mechanism with catalytic cycle including two half-reactions, overview. Proton transfer to His502 acting as a base, His546 plays a role in alcohol binding. Phe501 forces O2 to approach the flavin C4a, and His502 yielding hydrogen peroxide and the reoxidized flavin
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
modeling protein-ligand recognition mechanisms, substrate diffusion into the AAO active site, two conserved histidine residues, His502 and His546, are involved in catalysis, structure-function analysis, overview
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
oxidation mechanism by AAO, overview
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
two conserved histidine residues, His502 and His546, are involved in catalysis and play roles in the two half-reactions, with a stronger histidine involvement in the reductive than in the oxidative half-reaction. His502 is the catalytic base in the AAO reductive half-reaction. The His502 proton transfer does not limit the oxidative half-reaction, stereoselective hydride transfer. Quantum mechanical/molecular mechanical study, mutational analysis, and computational simulations, detailed overview
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
kinetic and reaction mechanisms involving residue Tyr92, hydride transfer reaction and aromatic stacking interactions on catalysis. Sequential reaction mechanism involving a ternary complex between AAO and its reducing/oxidizing substrates versus a ping-pong mechanism, overview
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, active site structure, Tyr92, Phe501, His502 and His546 are strictly required for activity, Tyr78 is not involved in catalysis, while Leu315 might be important
-
an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
9028-77-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
over 98% excess of the R enantiomer after treatment of racemic 1-(4-methoxyphenyl)ethanol, the hydride transfer is highly stereoselective
-
-
?
(S)-1-(4-methoxyphenyl)-ethanol + O2
1-(4-methoxyphenyl)acetaldehyde + H2O2
-
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
-
-
r
3,4-difluorobenzaldehyde + O2
3,4-difluorobenzoic acid + H2O2
-
-
-
?, r
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
ternary mechanism
-
-
?
3-chloro-4-anisyl alcohol + O2
3-chloro-4-anisaldehyde + H2O2
-
-
-
?
3-chloro-4-methoxybenzyl alcohol + O2
3-chloro-4-methoxybenzaldehyde + H2O2
ternary mechanism
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
r
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
-
-
-
r
5-(hydroxymethyl)furan-2-carboxylic acid + O2
2,5-furandicarboxylic acid + ?
very low activity
-
-
?
5-hydroxymethylfurfural + O2
5-(hydroxymethyl)furan-2-carboxylic acid + H2O2
-
-
-
?
(2E)-hept-2-en-1-ol + O2
(2E)-hept-2-enal + H2O2
31.9% of the activity with benzyl alcohol
-
-
?
(2E)-hex-2-en-1-ol + O2
(2E)-hex-2-enal + H2O2
63.9% of the activity with benzyl alcohol
-
-
?
(2E,4E)-hepta-2,4-dien-1-ol + O2
(2E,4E)-hepta-2,4-dienal + H2O2
737% of the activity with benzyl alcohol
-
-
?
(2E,4E)-hexa-2,4-dien-1-ol + O2
(2E,4E)-hexa-2,4-dienal + H2O2
807% of the activity with benzyl alcohol
-
-
?
(2H-1,3-benzodioxol-5-yl)methanol + O2
2H-1,3-benzodioxole-5-carbaldehyde + H2O2
301% of the activity with benzyl alcohol
-
-
?
(naphthalen-2-yl)methanol + O2
naphthalene-2-carbaldehyde + H2O2
874% of the activity with benzyl alcohol
-
-
?
(pyrene-1-yl)methanol + O2
pyrene-1-carbaldehyde + H2O2
35% of the activity with benzyl alcohol
-
-
?
(thiophen-2-yl)methanol + O2
thiophene-2-carbaldehyde + H2O2
15.8% of the activity with benzyl alcohol
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
177.5% of the activity with benzyl alcohol
-
?
2,4-hexadien-1-ol + O2
? + H2O2
-
531% of the activity with benzyl alcohol
-
?
2-naphthalenemethanol + O2
2-naphthaleneformaldehyde + H2O
-
745.7% of the activity with benzyl alcohol
-
?
3,4-dimethoxybenzyl alcohol + O2
3,4-dimethoxybenzaldehyde + H2O2
-
326.1% of the activity with benzyl alcohol
-
?
3,4-dimethoxybenzyl alcohol + O2
veratryl aldehyde + H2O2
-
i.e. veratryl alcohol
-
?
3-chloro-4-anisyl alcohol + O2
3-chloro-4-anisyl aldehyde + H2O2
-
high activity
-
-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzyl aldehyde + H2O2
-
low activity
-
-
?
3-methoxybenzyl alcohol + O2
3-methoxybenzaldehyde + H2O2
-
as active as benzyl alcohol
-
?
4-aminobenzyl alcohol + O2
4-aminobenzaldehyde + H2O2
18.6% of the activity with benzyl alcohol
-
-
?
anisyl alcohol + O2
anisyl aldehyde + H2O2
647% of the activity with benzyl alcohol
-
-
?
cinnamyl alcohol + O2
cinnamaldehyde + H2O2
-
451.1% of the activity with benzyl alcohol
-
?
cumic alcohol + O2
cumic aldehyde + H2O2
149% of the activity with benzyl alcohol
-
-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
-
-
-
?
(S)-1-(4-fluorophenyl)ethanol + O2
1-(4-fluorophenyl)acetaldehyde + H2O2
mutant F501A
-
-
?
2,5-diformylfuran + O2
formylfurancarboxylic acid + ?
-
-
-
?
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
-
-
r
3-chlorobenzyl alcohol + O2
3-chlorobenzaldehyde + H2O2
ping-pong mechanism
-
-
?
3-fluorobenzyl alcohol + O2
3-fluorobenzaldehyde + H2O2
ping-pong mechanism
-
-
?
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
high activity, 4-methoxybenzyl alcohol, is one of the best substrates of AAO, and 4-methoxybenzaldehyde (4-anisaldehyde) is the main extracellular aromatic metabolite in Pleurotus species
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
ternary mechanism
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzyl aldehyde + H2O2
-
-
-
?
5-hydroxymethylfurfural + O2
2,5-diformylfuran + H2O2
-
-
-
?
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
?
formylfurancarboxylic acid + O2
2,5-furandicarboxylic acid + H2O2
-
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
571.4% of the activity with benzyl alcohol
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, overview
-
-
?
cinnamyl alcohol + O2
cinnamyl aldehyde + H2O2
442% of the activity with benzyl alcohol
-
-
?
isovanillyl alcohol + O2
isovanillyl aldehyde + H2O2
246% of the activity with benzyl alcohol
-
-
?
veratryl alcohol + O2
veratryl aldehyde + H2O2
322% of the activity with benzyl alcohol
-
-
?
additional information
?
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
oxidation of aromatic and aliphatic polyunsaturated primary alcohols by wild-type and recombinant enzymes, overview
-
-
?
additional information
?
-
-
oxidation of aromatic and aliphatic polyunsaturated primary alcohols by wild-type and recombinant enzymes, overview
-
-
?
additional information
?
-
AAO typically oxidizes aromatic alcohols to the corresponding aldehydes. However, the enzyme can also oxidize aromatic aldehydes to the corresponding acids
-
-
?
additional information
?
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
substrate specificity, overview. AAO also shows some activity on aromatic aldehydes, the highest activity on 4-nitrobenzaldehyde being about 5% of the activity for benzyl alcohol. Extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids, AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds
-
-
?
additional information
?
-
-
substrate specificity, overview. AAO also shows some activity on aromatic aldehydes, the highest activity on 4-nitrobenzaldehyde being about 5% of the activity for benzyl alcohol. Extracellular AAO oxidizes aryl alcohols to aldehydes and eventually to acids, AAO efficiently oxidizes phenolic benzylic alcohols, e.g. benzylic, p-methoxybenzylic, veratrylic, and vanillylic compounds
-
-
?
additional information
?
-
the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid
-
-
?
additional information
?
-
the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
-
-
?
additional information
?
-
enzyme AAO is also able to oxidize some furanic compounds such as 5-hydroxymethylfurfural (HMF) and 2,5-diformylfuran (DFF), it has very low activity on 2,5-hydroxymethylfurancarboxylic acid, no activity with 2,5-formylfurancarboxylic acid. NMR analysis of the compounds
-
-
?
additional information
?
-
the enzyme shows a T-shaped stacking interaction between the Tyr92 side chain and the alcohol substrate at the catalytically competent position for concerted hydride and proton transfers. Bi-substrate kinetics analysis reveals that reactions with 3-chloro- or 3-fluorobenzyl alcohols (halogen substituents) proceed via a ping-pong mechanism. But mono- and dimethoxylated substituents (in 4-methoxybenzyl and 3,4-dimethoxybenzyl alcohols) alter the mechanism and a ternary complex is formed. Stacking energies, reaction mechanism, and kinetic analysis, role of Tyr92 in substrate binding and governing the kinetic mechanism in AAO, overview. Tyr-substrate binding energy and active site structure
-
-
?
additional information
?
-
for complete oxidation of 5-hydroxymethylfurfural, the rate-limiting step lies in the final oxidation of the intermediate 5-formyl-furancarboxylic acid to 2,5-furandicarboxylic acid. Wild-type AAO is not able to catalyze 5-formyl-furancarboxylic acid oxidation
-
-
-
additional information
?
-
-
no activity with aliphatic and secondary aromatic alcohols
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
4-(hydroxymethyl)-benzoic acid is a poor substrate
-
-
?
additional information
?
-
-
an H2O2-producing ligninolytic enzyme, molecular docking study of substrates, overview
-
-
?
additional information
?
-
-
AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
-
-
?
additional information
?
-
-
during catalysis the non-covalently bound FAD cofactor is reduced by the substrate and subsequently reoxidized by molecular oxygen to yield hydrogen peroxide. The AAO substrate-binding pocket is located on the si side of the flavin ring and connected to the exposed surface by a hydrophobic substrate access channel. Two putative catalytic histidines, H502 and H546, are essential in AAO activity as a possible general bases in AAO catalysis. Residue F501, located near of cofactor and the putative catalytic histidines, is also involved in substrate oxidation by AAO
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate specificity and highly stereoselective reaction mechanism. Assay method using ABTS [2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)]/horseradish peroxidase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,S)-4-methoxybenzyl alcohol + O2
1-(4-methoxyphenyl)ethanol + H2O2
over 98% excess of the R enantiomer after treatment of racemic 1-(4-methoxyphenyl)ethanol, the hydride transfer is highly stereoselective
-
-
?
2,4-dimethoxybenzyl alcohol + O2
2,4-dimethoxybenzaldehyde + H2O2
-
-
-
r
2-naphthylmethanol + O2
2-naphthaldehyde + H2O2
best substrate
-
-
r
4-anisyl alcohol + O2
4-anisaldehyde + H2O2
the substrate is an extracellular fungal metabolite
-
-
?
4-anisyl alcohol + O2
4-anisyl aldehyde + H2O2
preferred substrate
-
-
?
4-hydroxy-3-methoxybenzyl alcohol + O2
4-hydroxy-3-methoxybenzaldehyde + H2O2
-
-
-
r
4-methoxycinnamyl alcohol + O2
4-methoxycinnamaldehyde + H2O2
-
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
-
-
-
?
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
high activity, 4-methoxybenzyl alcohol, is one of the best substrates of AAO, and 4-methoxybenzaldehyde (4-anisaldehyde) is the main extracellular aromatic metabolite in Pleurotus species
-
-
r
4-methoxybenzyl alcohol + O2
4-methoxybenzaldehyde + H2O2
i.e. 4-anisyl alcohol
-
-
?
additional information
?
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
-
the enzyme provides H2O2 for fungal degradation of lignin
-
-
?
additional information
?
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
-
AAO substrates in lignin degradation can include both lignin-derived compounds and aromatic fungal metabolites. The former are phenolic aromatic aldehydes and acids being reduced to alcohol substrates by aryl-alcohol dehydrogenases (EC 1.1.1.90) and aryl-aldehyde dehydrogenases (E.C.1.2.1.29) , respectively
-
-
?
additional information
?
-
the ability of fungal aryl-alcohol oxidase (AAO) to oxidize 5-hydroxymethylfurfural (HMF) results in almost complete conversion into 2,5-formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5-diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. AAO is combined with an unspecific peroxygenase, UPO, EC 1.11.2.1, from Agrocybe aegerita for full oxidative conversion of 5-hydroxymethylfurfural in an enzymatic cascade. This peroxygenase belongs to the recently described superfamily of hemethiolate peroxidases, and is capable of incorporating peroxide-borne oxygen into diverse substrate molecules. In contrast to AAO, the UPO reaction starts with oxidation of the HMF carbonyl group, yielding 2,5-hydroxymethylfurancarboxylic, which is converted into 2,5-formylfurancarboxylic acid and some 2,5-furandicarboxylic acid
-
-
?
additional information
?
-
the enzyme typically catalyze the oxidative dehydrogenation of polyunsaturated alcohols using molecular oxygen as the final electron acceptor and producing hydrogen peroxide
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
the enzyme is involved in lignin degradation
-
-
?
additional information
?
-
-
AAO is able to catalyze the oxidative dehydrogenation of a wide range of aromatic and aliphatic primary polyunsaturated alcohols
-
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
4-methoxybenzylamine
-
uncompetitive, pH-dependent inhibition, best at pH 8.0
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
2,4-hexadienal
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
3
3,4-difluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.7
3-chloro-4-anisaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
1.5
3-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
2.2
3-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
4.7
4-Chlorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
4.9
4-Fluorobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
7
benzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
8
veratraldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.092
2,4-hexadien-1-ol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.095
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
0.22
3-anisyl alcohol
native enzyme, pH 6, temperature not specified in the publication
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
0.3
3-anisyl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
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
0.03
4-anisyl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.037
4-anisyl alcohol
pH 8.0, 25°C, recombinant enzyme from Escherichia coli
0.04
4-anisyl alcohol
native enzyme, pH 6, temperature not specified in the publication
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
3.6
4-methoxybenzyl alcohol
pH 6.0, 25°C, mutant F501A, oxidative half-reaction
2
4-nitrobenzaldehyde
mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
5
4-nitrobenzaldehyde
wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0
0.37
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
0.63
benzyl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.758
benzyl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
0.85
benzyl alcohol
native enzyme, pH 6, temperature not specified in the publication
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
native enzyme, pH 6, temperature not specified in the publication
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
0.56
veratryl alcohol
recombinant enzyme, pH 6, temperature not specified in the publication
0.59 - 1
veratryl alcohol
pH 8.0, 25°C, recombinant enzyme from Emericella nidulans
additional information
additional information
steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview
-
additional information
additional information
mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base
-
additional information
additional information
-
mechanism for alcohol oxidation, i.e the reductive half-reaction, and kinetics, including substrate and solvent kinetic isotope effects, hydride transfer from substrate Calpha to flavin N5 concerted with proton abstraction from alpha-hydroxyl by a catalytic base
-
additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of overall and half-reactions of wild-type and mutant enzymes by (anaerobic) stopped-flow spectrophotometry, changes in the flavin redox state, detailed overview
-
additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
steady state and transient state kinetic constants for alcohol and O2 of AAO oxidation of a deuterated and normal (alpha-protiated) 4-methoxybenzyl alcohol, solvent kinetic isotope effects, overview
-
additional information
additional information
steady-state and transient kinetics of overall reaction, and oxidative and reductive half-reactions, overview
-
additional information
additional information
steady-state and stopped-flow kinetics, bi-substrate kinetics analysis, kinetic mechanisms, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
stopped-flow and steady-state kinetics
-
additional information
additional information
-
MichaelisMenten kinetics and redox potentials of wild-type and mutant enzymes, overview
-
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
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
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
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
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
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
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
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
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
AAO shows no pH dependence of kcat or catalytic efficiency for the substrates analyzed, AAO is unstable above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
20°C: about 55% of maximal activity, 60°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
3.9
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
physiological function
additional information
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 by mixed quantum mechanics/molecular mechanics studies, overview
evolution
the enzyme belongs to the glucosemethanolcholine oxidase superfamily
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 H2O2 for lignin biodegradation
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 provides H2O2 to ligninolytic peroxidases
physiological function
the flavoenzyme aryl-alcohol oxidase is involved in lignin degradation
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
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 provides hydrogen peroxide necessary for peroxidase activity during lignin biodegradation
physiological function
-
aryl-alcohol oxidase (AAO) is an extracellular flavoprotein that supplies ligninolytic peroxidases with H2O2 during natural wood decay
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
docking of 4-methoxybenzyl alcohol at the buried crystal active site, and quantum mechanical/molecular mechanical study, overview
additional information
mixed quantum mechanics/molecular mechanics studies and molecular dynamics, 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
-
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
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). O94219_PLEER
593
0
63709
TrEMBL
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
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
?
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 * 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
?
-
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
monomer
1 * 100000, recombinant protein, 1 * 70000, PNGase F-treated protein, SDS-PAGE, 1 * 60800, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycoprotein
recombinant protein from wild-type Saccharomyces cerevisiae, 60% glycosylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 1 M Li2SO4, 0.1 M bis-Tris propane pH 7.4
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
H502A
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
H546S
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
synthesis
expression of AAO in the ascomycete Aspergillus nidulans. The activity of the recombinant enzyme in Aspergillus nidulans cultures is much higher than found in the extracellular fluid of Pleurotus eryngii. The recombinant enzyme shows the same molecular mass, pI and catalytic properties as that of the mature protein secreted by Pleurotus eryngii
Y92F
Y92L
Y92W
F501A
F501Y
H502R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H546R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
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
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
additional information
F501A
site-directed mutagenesis, the mutant shows strongly reduced O2 reactivity compared to the wild-type enzyme
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
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
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
mutant with increased activity on 5-hydroxymethylfurfural and its oxidation products
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
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
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 wild-type and mutant emzymes from Escherichia coli to homogeneity
recombinant enzyme from Emericella nidulans by gel filtration and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, recombinant expression in Escherichia coli
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
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
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 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, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the non-glycosylated recombinant enzyme is successfully activated in vitro after Escherichia coli expression in form of inclusion bodies
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
expression and secretion of AAO with yield of 315 mg/l using Pichia pastoris
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
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
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
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
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
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
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)
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
-
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
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)
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
Bjerkandera adusta, Botrytis cinerea, Phanerodontia chrysosporium, Trametes versicolor, Rigidoporus microporus, Fusarium solani, Postia placenta, Pleurotus eryngii (O94219), Pleurotus eryngii
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)
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)
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)
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)
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
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)
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)
-
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)
-
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
Varela, E.; Guillen, F.; Martinez, A.T.; Martinet, 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 (O94219), Pleurotus eryngii
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)
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)
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
EXTERNAL LINKS (specific for EC-Number 1.1.3.7)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
