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
-
polycrystalline
-
remazol
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glucose-methanol-choline
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president
-
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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KM Value
KM Value on EC 1.1.3.7 - aryl-alcohol oxidase
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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
-
protein fused to peroxidase, linker (GGGGS)17, pH 4, 25°C
0.0214
(R,S)-4-methoxybenzyl alcohol
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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
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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
0.22
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
4.91
3-Methoxybenzyl alcohol
recombinant enzyme, at pH 6.0 and 30°C
0.7
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
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
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
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
0.63
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
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
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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stopped-flow and steady-state kinetics
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additional information
additional information
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MichaelisMenten kinetics and redox potentials of wild-type and mutant enzymes, overview
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additional information
additional information
steady and pre-steady state kinetics and primary and solvent isotope effects of the substrates, overview
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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
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additional information
additional information
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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
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additional information
additional information
Michaelis-Menten steady-state and transient-state kinetics of wild-type and mutant enzymes, overview
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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
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additional information
additional information
steady-state and transient kinetics of overall reaction, and oxidative and reductive half-reactions, overview
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additional information
additional information
steady-state and stopped-flow kinetics, bi-substrate kinetics analysis, kinetic mechanisms, overview
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