1.1.3.7: aryl-alcohol oxidase
This is an abbreviated version!
For detailed information about aryl-alcohol oxidase, go to the full flat file.
Word Map on EC 1.1.3.7
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1.1.3.7
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anodic
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aluminum
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fabric
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nanoporous
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porous
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film
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nanostructures
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ascending
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aorta
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lignin
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nanowires
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nanotube
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laccase
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etch
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nanochannels
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ophthalmology
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age-at-onset
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academy
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decolor
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nanorods
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pleurotus
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ligninolytic
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white-rot
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bicuspid
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free-standing
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eryngii
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electrodeposition
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sputter
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valsalva
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large-area
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template-assisted
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environmental protection
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synthesis
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aortopathy
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bjerkandera
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nanopillars
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four-dimensional
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nanopatterns
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photovoltaic
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polycrystalline
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remazol
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glucose-methanol-choline
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president
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nanoarrays
- 1.1.3.7
-
anodic
-
aluminum
-
fabric
-
nanoporous
-
porous
-
film
-
nanostructures
-
ascending
-
aorta
- lignin
-
nanowires
-
nanotube
- laccase
-
etch
-
nanochannels
-
ophthalmology
-
age-at-onset
-
academy
-
decolor
-
nanorods
- pleurotus
-
ligninolytic
-
white-rot
-
bicuspid
-
free-standing
- eryngii
-
electrodeposition
-
sputter
-
valsalva
-
large-area
-
template-assisted
- environmental protection
- synthesis
-
aortopathy
- bjerkandera
-
nanopillars
-
four-dimensional
-
nanopatterns
-
photovoltaic
-
polycrystalline
-
remazol
-
glucose-methanol-choline
-
president
-
nanoarrays
Reaction
Synonyms
AAO, AAO2, AAOx, alcohol: O2 oxidoreductase, AOX, arom. alcohol oxidase, aryl alcohol oxidase, arylalcohol oxidase, CpSAO, CtSAO, GaoB, GLRG_02805, GMC oxidoreductase-like protein, HMFO, More, MtGloA, MYCTH_2299749, oxidase, aryl alcohol, salicyl alcohol oxidase, um04044, VAO, veratryl alcohol oxidase
ECTree
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General Information
General Information on EC 1.1.3.7 - aryl-alcohol oxidase
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evolution
metabolism
physiological function
additional information
the enzyme belongs to the glucose methanol choline oxidase superfamily
evolution
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the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
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the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
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the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview
evolution
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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
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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
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
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aryl-alcohol oxidase provides hydrogen peroxide necessary for peroxidase activity during lignin biodegradation
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
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aryl alcohol oxidase is involved in lignin degradation
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
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the enzyme is part of the extracellular enzymatic machinery of the fungus to degrade lignin. The secreted, extracellular oxidase generates H2O2 for extracellular peroxidases
physiological function
the enzyme is part of the extracellular enzymatic machinery of the fungus to degrade lignin. The secreted, extracellular oxidase generates H2O2 for extracellular peroxidases. O2 activation by Pleurotus eryngii AAO takes place during the redox-cycling of 4-methoxylated benzylic metabolites secreted by the fungus. AAO provides a continuous supply of H2O2 by redox cycling phenolic benzylic alcohol compounds, in collaboration with mycelium dehydrogenases
physiological function
the enzyme provides H2O2 to ligninolytic peroxidases
physiological function
the flavoenzyme aryl-alcohol oxidase is involved in lignin degradation
physiological function
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aryl-alcohol oxidase (AAO) is an extracellular flavoprotein that supplies ligninolytic peroxidases with H2O2 during natural wood decay
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
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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
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
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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
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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
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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
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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