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
-
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
- 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
1.1.3.7 aryl-alcohol oxidaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.3.7 - aryl-alcohol oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
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
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
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
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 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
-
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
-
