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(R)-1,2-propanediol + O2
? + H2O2
-
-
-
?
(R)-2-octanol + O2
2-octanone + H2O2
-
-
-
-
?
(R)-2-octanol + O2
octan-2-one + H2O2
1,2-ethanediol + O2
?
-
-
-
-
?
1,2-propanediol + O2
? + H2O2
-
-
-
-
?
1,3-butylene glycol + O2
? + H2O2
1,4-butynediol + O2
4-hydroxy-2-butyn-1-al + H2O2
-
oxidized to mechanism-based irreversible inactivator: 4-hydroxy-2-butynal
mechanism-based inhibitor
?
1-butanol + O2
butanal + H2O2
1-butanol + O2
butanaldehyde + H2O2
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
1-butanol + O2
n-butanal + H2O2
1-decanol + O2
decanal + H2O2
1-heptanol + O2
heptanal + H2O2
-
-
-
?
1-hexanol + O2
hexanal + H2O2
1-hexanol + O2 + H2O
hexanal + H2O2
-
-
-
?
1-octanol + O2
n-octanal + H2O2
1-octanol + O2
octanal + H2O2
1-pentanol + O2
n-pentanal + H2O2
1-pentanol + O2
pentanal + H2O2
1-pentanol + O2
pentanaldehyde + H2O2
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
1-propanol + O2
n-propanal + H2O2
1-propanol + O2
propanal + H2O2
1-tetradecanol + O2
tetradecanal + H2O2
-
-
-
?
1-undecanol + O2
undecanal + H2O2
2 5-aminopentan-1-ol + O2
5-(piperidin-2-yl)-2,3,4,5-tetrahydropyridine + H2O2
-
-
-
?
2,2'-sulfanediyldi(ethan-1-ol) + O2
[(2-hydroxyethyl)sulfanyl]acetic acid + H2O2
-
-
-
?
2,2'-[ethane-1,2-diylbis(oxy)]di(ethan-1-ol) + O2
[2-(2-oxoethoxy)ethoxy]acetic acid + H2O2
-
-
-
?
2-butanol + O2
2-butanone + H2O2
2-buten-1-ol + O2
2-buten-1-al + H2O2
-
-
-
-
?
2-chloroethanol + O2
2-chloroethanal + H2O2
-
66% of the activity with methanol
-
-
?
2-cyanoethanol + O2
2-cyanoethanal + H2O2
-
30% of the activity with methanol
-
-
?
2-dodecanol + O2
dodecan-2-one + H2O2
2-mercaptoethanol + O2
2-mercaptoethanal + H2O2
2-methoxyethanol + O2
2-methoxyethanal + H2O2
-
40% of the activity with methanol
-
-
?
2-methyl-1-butanol
2-methylbutanal + H2O2
-
-
-
-
?
2-methyl-1-butanol + O2
2-methyl-1-butanal + H2O2
-
22% of the activity with methanol
-
-
?
2-methyl-1-hexanol
2-methylhexanal + H2O2
-
-
-
-
?
2-methyl-1-pentanol
2-methylpentanal + H2O2
-
-
-
-
?
2-methyl-1-propanol + O2
butan-2-one + H2O2
7% of the activity with methanol
-
-
?
2-methyl-2-propanol + O2
?
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
2-propanol + O2
2-oxopropane + H2O2
-
-
-
-
?
2-propanol + O2
acetone + H2O2
2-propen-1-ol + O2
2-propen-1-al + H2O2
2-propyn-1-ol + O2
2-propyn-1-al + H2O2
Poria contigua
-
-
-
-
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
3-buten-1-ol + O2
but-3-enal + H2O2
-
-
-
-
?
3-chloro-1-propanol + O2
3-chloro-1-propanal + H2O2
-
22% of the activity with methanol
-
-
?
3-methyl-1-butanol + O2
3-methylbutanal + H2O2
7% of the activity with methanol
-
-
?
3-phenylpropan-1-ol + O2
3-phenylpropanal + H2O2
4-chloro-1-butanol + O2
4-chloro-1-butanal + H2O2
-
11% of the activity with methanol
-
-
?
4-hepten-1-ol + O2
4-hepten-1-al + H2O
-
-
-
?
4-nonen-1-ol + O2
4-nonen-1-al + H2O2
-
-
-
?
4-penten-1-ol + O2
pent-4-enal + H2o2
-
-
-
-
?
allylalcohol + O2
acrolein + H2O2
arabitol + O2
?
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
bromoethanol + O2
bromoethanal + H2O2
-
4% of the activity with methanol
-
-
?
butan-1-ol + O2
n-butanal + H2O2
butane-1,4-diol + O2
oxolan-2-one + H2O2
-
-
-
?
chloroethanol + O2
chloroethanal + H2O2
crotyl alcohol + O2
(2E)-but-2-enal + H2O2
-
-
-
-
?
cyclohexanol + O2
cyclohexanal + H2O2
D-ribose + O2
? + H2O2
-
-
-
-
?
decanol + O2
decanal + H2O2
-
-
-
-
?
diethylene glycol + 2 O2
2-(2-hydroxyethoxy)acetic acid + H2O2
-
-
-
?
dodecanol + O2
dodecanal + H2O2
-
-
-
-
?
erythritol + O2
? + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
ethylene glycol + O2
? + H2O2
ethylene glycol mono-methylether + O2
methoxyacetaldehyde + H2O2
formaldehyde + methylene blue
formic acid + ?
-
-
-
-
?
formaldehyde + O2
formate + H2O2
formaldehyde + O2
formic acid + H2O2
formaldehyde + p-benzoquinone
formic acid + p-benzoquinol
-
p-benzoquinone, having the highest redox potential, proves to be the most efficient artificial electron acceptor
-
-
?
formaldehyde + toluidine blue
formic acid + ?
-
-
-
-
?
glucose + O2
? + H2O2
-
-
-
-
?
glycerol + O2
? + H2O2
-
-
-
-
?
glycerol + O2
glyceraldehyde + H2O2
glycolate + O2
glyoxylate + H2O2
-
100% activity
-
-
?
hexadecanol + O2
hexadecanal + H2O2
hexan-1-ol + O2
hexanoic acid + H2O2
-
-
-
?
hexane-1,6-diol + O2
6-oxohexanoic acid + cyclopent-1-ene-1-carbaldehyde + H2O2
-
-
-
?
hexanol + O2
hexanal + H2O2
hydroxyquinone + O2
?
-
-
-
-
?
isoamyl alcohol + O2
3-methylbutanal + H2O2
-
-
-
-
?
isoamyl alcohol + O2
? + H2O2
-
2% of the activity with methanol
-
-
?
isobutanol + O2
isobutanal + H2O2
isobutanol + O2
isobutyraldehyde + H2O2
isopropanol + O2
2-propanone + H2O2
L-tryptophan + O2
?
-
-
-
-
?
lactate + O2
decanal + H2O2
-
14% activity compared to glycolate
-
-
?
methanol + O2
formaldehyde + H2O2
n-butanol + O2
butanal + H2O2
n-butanol + O2
butanaldehyde + H2O2
-
-
-
-
?
n-butanol + O2
butyraldehyde + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
n-dodecanol + O2
n-dodecanal + H2O2
n-heptanol + O2
heptanal + H2O2
n-heptanol + O2
heptanaldehyde + H2O2
-
-
-
-
?
n-heptanol + O2
n-heptanal + H2O2
n-hexanol + O2
n-hexanal + H2O2
n-octanol + O2
octanaldehyde + H2O2
-
-
-
-
?
n-pentanol + O2
n-pentanal + H2O2
n-propanol + O2
n-propanal + H2O2
n-propanol + O2
propanal + H2O2
-
-
-
-
?
n-propanol + O2
propanaldehyde + H2O2
n-propanol + O2
propionaldehyde + H2O2
octane-1,8-diol + O2
6-oxooctanoic acid + H2O2
-
-
-
?
pentan-1-ol + O2
pentanal + H2O2
-
50% of the activity with methanol
-
-
?
pentan-2-ol + O2
pentanone + H2O2
-
56% of the activity with methanol
-
-
?
pentane-1,4-diol + O2
5-methyloxolan-2-one + H2O2
-
-
-
?
pentane-1,5-diol + O2
5-hydroxypentanoic acid + H2O2
-
-
-
?
phenyl-3-propanol + O2
3-phenylpropanal
-
-
-
-
?
prop-2-en-1-ol + O2
acrylaldehyde + H2O2
-
81% of the activity with methanol
-
-
?
propargyl alcohol + O2
propargyl aldehyde + H2O2
propylene glycol + O2
?
-
low activity with intra- and extracellular enzymes
-
-
?
R-(2)-octanol + O2
octan-2-one + H2O2
-
-
-
-
?
rac-1-phenylethanol + O2
acetophenone + H2O2
-
-
-
-
?
ribitol + O2
? + H2O2
-
-
-
-
?
tetradecanol + O2
tetradecanal + H2O2
-
-
-
-
?
xylidine + O2
?
-
lowest specific activity with xylidine
-
-
?
additional information
?
-
(R)-2-octanol + O2
octan-2-one + H2O2
-
-
-
-
?
(R)-2-octanol + O2
octan-2-one + H2O2
-
-
-
-
?
1,3-butylene glycol + O2
? + H2O2
-
-
-
-
?
1,3-butylene glycol + O2
? + H2O2
-
-
-
-
?
1-butanol + O2
butanal + H2O2
-
373% activity compared to glycolate
-
-
?
1-butanol + O2
butanal + H2O2
-
-
-
-
?
1-butanol + O2
butanal + H2O2
-
-
-
?
1-butanol + O2
butanal + H2O2
-
-
-
-
?
1-butanol + O2
n-butanal + H2O2
-
49% of the activity with methanol
-
-
?
1-butanol + O2
n-butanal + H2O2
-
49% of the activity with methanol
-
-
?
1-butanol + O2
n-butanal + H2O2
54% of the activity with methanol
-
-
?
1-decanol + O2
decanal + H2O2
-
-
-
?
1-decanol + O2
decanal + H2O2
-
180% activity compared to glycolate
-
-
?
1-hexanol + O2
hexanal + H2O2
-
-
-
?
1-hexanol + O2
hexanal + H2O2
-
300% activity compared to glycolate
-
-
?
1-hexanol + O2
hexanal + H2O2
-
-
-
-
?
1-octanol + O2
n-octanal + H2O2
-
-
-
-
?
1-octanol + O2
n-octanal + H2O2
-
2.4% of the activity with methanol
-
-
?
1-octanol + O2
octanal + H2O2
-
-
-
?
1-octanol + O2
octanal + H2O2
-
189% activity compared to glycolate
-
-
?
1-octanol + O2
octanal + H2O2
-
-
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
1% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
21% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
21% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
22% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
30% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
33.5% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
33.5% of the activity with methanol
-
-
?
1-pentanol + O2
pentanal + H2O2
-
448% activity compared to glycolate
-
-
?
1-pentanol + O2
pentanal + H2O2
-
-
-
-
?
1-pentanol + O2
pentanal + H2O2
-
-
-
?
1-pentanol + O2
pentanal + H2O2
-
-
-
-
?
1-propanol + O2
n-propanal + H2O2
-
66% of the activity with methanol
-
-
?
1-propanol + O2
n-propanal + H2O2
-
66% of the activity with methanol
-
-
?
1-propanol + O2
n-propanal + H2O2
73% of the activity with methanol
-
-
?
1-propanol + O2
n-propanal + H2O2
27% activity compared to methanol
-
-
?
1-propanol + O2
n-propanal + H2O2
-
27% activity compared to methanol
-
-
?
1-propanol + O2
propanal + H2O2
-
-
-
?
1-propanol + O2
propanal + H2O2
-
63% activity compared to glycolate
-
-
?
1-propanol + O2
propanal + H2O2
-
-
-
-
?
1-propanol + O2
propanal + H2O2
-
-
-
?
1-propanol + O2
propanal + H2O2
-
-
-
-
?
1-propanol + O2
propanal + H2O2
-
-
-
?
1-undecanol + O2
undecanal + H2O2
-
-
-
-
?
1-undecanol + O2
undecanal + H2O2
-
-
-
-
?
2-butanol + O2
2-butanone + H2O2
-
3.5% of the activity with methanol
-
-
?
2-butanol + O2
2-butanone + H2O2
-
3.5% of the activity with methanol
-
-
?
2-dodecanol + O2
dodecan-2-one + H2O2
-
-
-
-
?
2-dodecanol + O2
dodecan-2-one + H2O2
-
-
-
-
?
2-mercaptoethanol + O2
2-mercaptoethanal + H2O2
-
25% of the activity with methanol
-
-
?
2-mercaptoethanol + O2
2-mercaptoethanal + H2O2
Poria contigua
-
-
-
-
?
2-propanol + O2
acetone + H2O2
-
low activity with the extracellular enzyme
-
-
?
2-propanol + O2
acetone + H2O2
-
low activity with the extracellular enzyme
-
-
?
2-propen-1-ol + O2
2-propen-1-al + H2O2
-
17% of the activity with methanol
-
-
?
2-propen-1-ol + O2
2-propen-1-al + H2O2
-
82% of the activity with methanol
-
-
?
2-propen-1-ol + O2
2-propen-1-al + H2O2
-
-
in vivo leads to cell intoxination
?
2-propen-1-ol + O2
2-propen-1-al + H2O2
-
-
-
-
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
-
45% of the activity with methanol
-
-
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
Poria contigua
-
-
-
-
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
-
oxidized to mechanism-based irreversible inactivator: propynal
mechanism-based inhibitor
?
3-phenylpropan-1-ol + O2
3-phenylpropanal + H2O2
-
-
-
-
?
3-phenylpropan-1-ol + O2
3-phenylpropanal + H2O2
-
-
-
-
?
allylalcohol + O2
acrolein + H2O2
93% of the activity with methanol
-
-
?
allylalcohol + O2
acrolein + H2O2
-
-
-
-
?
allylalcohol + O2
acrolein + H2O2
-
-
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
9% of the activity with methanol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
81.3% of the activity with methanol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
21.3% of the activity with methanol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
21.3% of the activity with methanol
-
-
?
butan-1-ol + O2
n-butanal + H2O2
-
-
-
-
?
butan-1-ol + O2
n-butanal + H2O2
-
-
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
6% of the activity with methanol
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
6% of the activity with
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
2-chloroethanol, 70% of the activity with methanol
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
-
-
-
?
cyclohexanol + O2
cyclohexanal + H2O2
-
-
-
-
?
cyclohexanol + O2
cyclohexanal + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
very low activity in cells grown on n-hexadecane
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
28% of the activity with methanol
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
82% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
82% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
94% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
82% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
83% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
82% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
10% activity compared to glycolate
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97.2% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
106% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
106% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
92% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
60% activity compared to methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
60% activity compared to methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
92% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
Pichia putida
-
92% activity compared to methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
92% of the activity with methanol
-
?
ethanol + O2
acetaldehyde + H2O2
Polyporus obtusus
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
Poria contigua
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97.8% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97.8% of the activity with methanol
-
-
?
ethylene glycol + O2
?
-
12% of the activity with methanol
-
-
?
ethylene glycol + O2
?
-
12% of the activity with methanol
-
-
?
ethylene glycol + O2
?
-
9.2% of the activity with methanol
-
-
?
ethylene glycol + O2
?
-
1.7% of the activity with methanol
-
-
?
ethylene glycol + O2
?
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
ethylene glycol + O2
? + H2O2
-
-
-
-
?
ethylene glycol + O2
? + H2O2
-
-
-
-
?
ethylene glycol + O2
? + H2O2
-
-
-
-
?
ethylene glycol mono-methylether + O2
methoxyacetaldehyde + H2O2
-
10% of the activity with methanol
-
-
?
ethylene glycol mono-methylether + O2
methoxyacetaldehyde + H2O2
-
-
-
-
?
formaldehyde + O2
formate + H2O2
-
23% of the activity with methanol
-
?
formaldehyde + O2
formate + H2O2
-
-
-
?
formaldehyde + O2
formate + H2O2
-
-
-
-
?
formaldehyde + O2
formate + H2O2
Pichia putida
-
35% activity compared to methanol
-
-
?
formaldehyde + O2
formate + H2O2
-
15% of the activity with methanol
-
?
formaldehyde + O2
formate + H2O2
Poria contigua
-
-
-
-
?
formaldehyde + O2
formate + H2O2
-
-
-
?
formaldehyde + O2
formate + H2O2
-
-
-
?
formaldehyde + O2
formic acid + H2O2
-
-
-
-
?
formaldehyde + O2
formic acid + H2O2
-
-
-
-
?
formaldehyde + O2
formic acid + H2O2
-
low activity
-
-
?
formaldehyde + O2
formic acid + H2O2
-
28% of the activity with methanol
-
-
?
formaldehyde + O2
formic acid + H2O2
-
28% of the activity with methanol
-
-
?
formaldehyde + O2
formic acid + H2O2
-
-
-
-
?
formaldehyde + O2
formic acid + H2O2
-
-
-
-
?
glycerol + O2
glyceraldehyde + H2O2
17% activity compared to methanol
-
-
?
glycerol + O2
glyceraldehyde + H2O2
-
17% activity compared to methanol
-
-
?
hexadecanol + O2
hexadecanal + H2O2
-
-
-
-
?
hexadecanol + O2
hexadecanal + H2O2
-
62% of the activity with methanol
-
-
?
hexanol + O2
hexanal + H2O2
-
-
-
-
?
hexanol + O2
hexanal + H2O2
-
-
-
-
?
indole + O2
?
-
-
-
-
?
isobutanol + O2
isobutanal + H2O2
-
21% of the activity with methanol
-
-
?
isobutanol + O2
isobutanal + H2O2
-
2% of the activity with methanol
-
-
?
isobutanol + O2
isobutyraldehyde + H2O2
-
1.2% of the activity with methanol
-
-
?
isobutanol + O2
isobutyraldehyde + H2O2
-
no activity
-
-
?
isopropanol + O2
2-propanone + H2O2
-
21% of the activity with methanol
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
-
6.9% of the activity with methanol
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
Poria contigua
-
-
-
-
?
L-DOPA + O2
?
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
very low activity in cells grown on n-hexadecane
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
best substrate
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
possible role for AOX as a major source of H2O2
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
best substrate
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
alcohol oxidase is a key enzyme involved in the dissimilation of methanol
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
enzyme expression is tightly regulated, three regulatory sequences are involved
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
100% activity
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
100% activity
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
Pichia putida
-
100% activity
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
Polyporus obtusus
-
-
-
?
methanol + O2
formaldehyde + H2O2
Polyporus obtusus
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
Poria contigua
-
-
-
?
methanol + O2
formaldehyde + H2O2
Poria contigua
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
n-butanol + O2
butanal + H2O2
-
-
-
-
?
n-butanol + O2
butanal + H2O2
-
67% of the activity with methanol
-
-
?
n-butanol + O2
butanal + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
2.1% of the activity with methanol
-
?
n-butanol + O2
n-butanal + H2O2
-
2.1%, of the activity with methanol
-
?
n-butanol + O2
n-butanal + H2O2
-
27% of the activity with methanol
-
-
?
n-butanol + O2
n-butanal + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
20% of the activity with methanol
-
-
?
n-butanol + O2
n-butanal + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
57.2% of the activity with methanol
-
-
?
n-butanol + O2
n-butanal + H2O2
-
10.6% of the activity with methanol
-
-
?
n-butanol + O2
n-butanal + H2O2
-
10.6% of the activity with methanol
-
-
?
n-butanol + O2
n-butanal + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
Pichia putida
-
40% activity compared to methanol
-
-
?
n-butanol + O2
n-butanal + H2O2
-
52%, of the activity with methanol
-
?
n-butanol + O2
n-butanal + H2O2
Poria contigua
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
52.2% of the activity with methanol
-
-
?
n-dodecanol + O2
n-dodecanal + H2O2
-
-
-
-
?
n-dodecanol + O2
n-dodecanal + H2O2
-
-
-
-
?
n-heptanol + O2
heptanal + H2O2
-
-
-
-
?
n-heptanol + O2
heptanal + H2O2
-
-
-
-
?
n-heptanol + O2
n-heptanal + H2O2
-
-
-
-
?
n-heptanol + O2
n-heptanal + H2O2
-
substrates with highest affinity
-
-
?
n-heptanol + O2
n-heptanal + H2O2
-
-
-
-
?
n-hexanol + O2
n-hexanal + H2O2
-
-
-
-
?
n-hexanol + O2
n-hexanal + H2O2
-
4% of the activity with methanol
-
-
?
n-hexanol + O2
n-hexanal + H2O2
-
6.3% of the activity with methanol
-
-
?
n-pentanol + O2
n-pentanal + H2O2
-
-
-
-
?
n-pentanol + O2
n-pentanal + H2O2
13% activity compared to methanol
-
-
?
n-pentanol + O2
n-pentanal + H2O2
-
13% activity compared to methanol
-
-
?
n-pentanol + O2
n-pentanal + H2O2
Pichia putida
-
3% activity compared to methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
5.3% of the activity with methanol
-
?
n-propanol + O2
n-propanal + H2O2
-
38% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
38% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
maximum specific activity with n-propanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
maximum specific activity with n-propanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
43% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
43% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
72.2% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
33% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
33% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
Pichia putida
-
75% activity compared to methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
Poria contigua
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
77.5% of the activity with methanol
-
-
?
n-propanol + O2
propanaldehyde + H2O2
-
-
-
-
?
n-propanol + O2
propanaldehyde + H2O2
-
-
-
-
?
n-propanol + O2
propionaldehyde + H2O2
-
-
-
-
?
n-propanol + O2
propionaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
propargyl alcohol + O2
propargyl aldehyde + H2O2
-
-
-
-
?
propargyl alcohol + O2
propargyl aldehyde + H2O2
-
90% of the activity with methanol
-
-
?
veratryl alcohol + O2
?
-
-
-
-
?
veratryl alcohol + O2
?
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
additional information
?
-
-
substrate specificity dependent on growth substrate, overview
-
-
?
additional information
?
-
-
substrate specificity of native, intermediate dissociated protein and re-associated protein, overview
-
-
?
additional information
?
-
-
substrate specificity dependent on growth substrate, overview
-
-
?
additional information
?
-
-
substrate specificity of native, intermediate dissociated protein and re-associated protein, overview
-
-
?
additional information
?
-
-
FAO1 is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism, overview
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate range, D-glucose, 2-propanol, and ethylene glycol are poor substrates, no activity with 1,2-butenediol
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with isobutanol, benzyl alcohol, and cyclohexanol
-
-
?
additional information
?
-
enzyme is able to oxidize 5-(hydroxymethyl)furfural, yielding furan-2,5-dicarbaldehyde, reaction of EC 1.1.3.47
-
-
-
additional information
?
-
enzyme is able to oxidize 5-(hydroxymethyl)furfural, yielding furan-2,5-dicarbaldehyde, reaction of EC 1.1.3.47
-
-
-
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme does not oxidize benzyl alcohol, glycolaldehyde, glyoxylate, ethylene glycol, glycerol, or methanol
-
-
?
additional information
?
-
-
enzyme also catalyzes the oxidation of glycolate to glyoxylate, reaction of EC 1.1.3.15. No substrate: glyoxylate
-
-
-
additional information
?
-
-
no activity with lactic acid, glycerol, and tert-butanol
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
no or poor activity with 1-butanol, 2-butanol, 3-butanol, isoamyl alcohol, 2-propanol, and 2,2,2-trichloroethanol
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
correlation of activity of peroxisomal catalase and AO isogenic form 1 under different conditions reveal common regulatory elements for genes AUG2 and CTA1
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
very poor substrates: 1-hexanol, 1-octanol, 2-propanol, t-butanol, 3-pentanol, 3-methyl-1-butanol, glycerol
-
-
-
additional information
?
-
-
very poor substrates: 1-hexanol, 1-octanol, 2-propanol, t-butanol, 3-pentanol, 3-methyl-1-butanol, glycerol
-
-
-
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
oxidizes short-chain primary alcohols and ethylene glycol in a medium containing not only methanol, but also ethanol, ethylene glycol, glycerol or glucose. No activity with 1,2-propanediol and 1,3-propanediol or acetaldehyde
-
-
?
additional information
?
-
-
oxidizes short-chain primary alcohols and ethylene glycol in a medium containing not only methanol, but also ethanol, ethylene glycol, glycerol or glucose. No activity with 1,2-propanediol and 1,3-propanediol or acetaldehyde
-
-
?
additional information
?
-
alcohol oxidase facilitates double and triple oxidations for a range of aliphatic diols. Depending on the diol substrate, the reaction results in formation of either lactones or hydroxy acids
-
-
-
additional information
?
-
-
alcohol oxidase facilitates double and triple oxidations for a range of aliphatic diols. Depending on the diol substrate, the reaction results in formation of either lactones or hydroxy acids
-
-
-
additional information
?
-
enzyme additionally acts on secondary alcohols, reaction of EC 1.1.3.18. By selective oxidation of the (S)-alcohols, the (R)-alcohols can be obtained in high enantiopurity
-
-
-
additional information
?
-
-
enzyme additionally acts on secondary alcohols, reaction of EC 1.1.3.18. By selective oxidation of the (S)-alcohols, the (R)-alcohols can be obtained in high enantiopurity
-
-
-
additional information
?
-
poor substrate: glycerol
-
-
-
additional information
?
-
-
poor substrate: glycerol
-
-
-
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
no substrates: 2-dodecanol, 2-tetradecanol, 7-tetradecanol, 2-hexadecanol or secondary alcohols
-
-
-
additional information
?
-
-
no substrates: 2-dodecanol, 2-tetradecanol, 7-tetradecanol, 2-hexadecanol or secondary alcohols
-
-
-
additional information
?
-
-
substrate specificities of intra- and extracellular enzymes, overview, no activity by both with 2-butanol, 2-methyl-1-propanol, and glycerol
-
-
?
additional information
?
-
-
substrate specificities of intra- and extracellular enzymes, overview, no activity by both with 2-butanol, 2-methyl-1-propanol, and glycerol
-
-
?
additional information
?
-
-
2-propyn-1-ol and methylene cyclopropyl alcohol are not suicide substrates
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-ethanediol + O2
?
-
-
-
-
?
2-methyl-1-butanol
2-methylbutanal + H2O2
-
-
-
-
?
2-methyl-1-hexanol
2-methylhexanal + H2O2
-
-
-
-
?
2-methyl-1-pentanol
2-methylpentanal + H2O2
-
-
-
-
?
3-buten-1-ol + O2
but-3-enal + H2O2
-
-
-
-
?
4-penten-1-ol + O2
pent-4-enal + H2o2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
formaldehyde + O2
formic acid + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
methanol + O2
formaldehyde + H2O2
n-butanol + O2
butanaldehyde + H2O2
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
-
-
-
?
n-heptanol + O2
heptanaldehyde + H2O2
-
-
-
-
?
n-octanol + O2
octanaldehyde + H2O2
-
-
-
-
?
n-pentanol + O2
n-pentanal + H2O2
-
-
-
-
?
n-propanol + O2
n-propanal + H2O2
-
-
-
-
?
additional information
?
-
ethanol + O2
acetaldehyde + H2O2
-
very low activity in cells grown on n-hexadecane
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
very low activity in cells grown on n-hexadecane
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
possible role for AOX as a major source of H2O2
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
alcohol oxidase is a key enzyme involved in the dissimilation of methanol
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
enzyme expression is tightly regulated, three regulatory sequences are involved
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
Polyporus obtusus
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
Poria contigua
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
-
-
-
?
additional information
?
-
-
FAO1 is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism, overview
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
correlation of activity of peroxisomal catalase and AO isogenic form 1 under different conditions reveal common regulatory elements for genes AUG2 and CTA1
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
additional information
?
-
AOD isozymes and second AOD genes distribute widely in several methylotrophic yeasts in the natural environment, and second AOD genes may have evolved as methylotrophic genes that can adapt to the environmental conditions of higher methanol concentrations
-
-
?
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Janssen, F.W.; Ruelius, H.W.
Alcohol oxidase, a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyethylene glycol
Biochim. Biophys. Acta
151
330-342
1968
Basidiomycota
brenda
Janssen, F.W.; Kerwin, R.M.; Ruelius, H.W.
Alcohol oxidase from basidiomycetes
Methods Enzymol.
41B
364-369
1975
Basidiomycota, Polyporus obtusus, Radulodon casearius, Basidiomycota B191039
brenda
Yamada, H.; Shin, K.C.; Kato, N.; Shimizu, S.; Tani, Y.
Purification and characterization of alcohol oxidase from Candida 25-A
Agric. Biol. Chem.
43
877-878
1979
Candida sp. (in: Saccharomycetales), Candida sp. (in: Saccharomycetales) 25-A
-
brenda
Bringer, S.; Sprey, B.; Sahm, H.
Purification and properties of alcohol oxidase from Poria contigua
Eur. J. Biochem.
101
563-570
1979
Poria contigua
brenda
Nichols, C.S.; Cromartie, T.H.
Irreversible inactivation of the flavoenzyme alcohol, oxidase with acetylenic alcohols
Biochem. Biophys. Res. Commun.
97
216-221
1980
[Candida] boidinii
brenda
Couderc, R.; Baratti, J.
Oxidation of methanol by the yeast, Pichia pastoris. Purification and properties of the alcohol oxidase
Agric. Biol. Chem.
44
2279-2289
1980
Ogataea angusta, Komagataella pastoris, Komagataella pastoris IFP 206
-
brenda
Patel, R.N.; Hou, C.T.; Laskin, A.I.; Derelanko, P.
Microbial oxidation of methanol: properties of crystallized alcohol oxidase from a yeast, Pichia sp
Arch. Biochem. Biophys.
210
481-488
1981
Pichia sp.
brenda
Sahm, H.; Schuette, H.; Kula, M.R.
Alcohol oxidase from Candida boidinii
Methods Enzymol.
89
424-428
1982
[Candida] boidinii
-
brenda
Geissler, J.; Ghisla, S.; Kroneck, P.M.H.
Flavin-dependent alcohol oxidase from yeast. Studies on the catalytic mechanism and inactivation during turnover
Eur. J. Biochem.
160
93-100
1986
[Candida] boidinii
brenda
Van der Klei, I.J.; Bystryck, L.V.; Harder, W.
Alcohol oxidase from Hansenula polymorpha CBS 4732
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Preparation of convection interaction media isobutyl disc monolithic column and its application to purification of secondary alcohol dehydrogenase and alcohol oxidase
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Physiological study and alcohol oxidase gene(s) of thermotolerant methylotrophic yeasts isolated in Thailand
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Shumakovich, G.P.; Shleev, S.V.; Morozova, O.V.; Gonchar, M.V.; Yaropolov, A.I.
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Characteristics of Gloeophyllum trabeum alcohol oxidase, an extracellular source of H2O2 in brown rot decay of wood
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Kondo, T.; Morikawa, Y.; Hayashi, N.
Purification and characterization of alcohol oxidase from Paecilomyces variotii isolated as a formaldehyde-resistant fungus
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Kumar, A.K.; Goswami, P.
Purification and properties of a novel broad substrate specific alcohol oxidase from Aspergillus terreus MTCC 6324
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Dmytruk, K.V.; Smutok, O.V.; Ryabova, O.B.; Gayda, G.Z.; Sibirny, V.A.; Schuhmann, W.; Gonchar, M.V.; Sibirny, A.A.
Isolation and characterization of mutated alcohol oxidases from the yeast Hansenula polymorpha with decreased affinity toward substrates and their use as selective elements of an amperometric biosensor
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Analysis of methanol-ethanol mixtures from falsified beverages using a dual biosensors amperometric system based on alcohol dehydrogenase and alcohol oxidase
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van der Heide, M.; Leao, A.N.; Van der Klei, I.J.; Veenhuis, M.
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Barsan, M.M.; Brett, C.M.
An alcohol oxidase biosensor using PNR redox mediator at carbon film electrodes
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Ogataea angusta
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Wu, L.; McIntosh, M.; Zhang, X.; Ju, H.
Amperometric sensor for ethanol based on one-step electropolymerization of thionine-carbon nanofiber nanocomposite containing alcohol oxidase
Talanta
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Ogataea angusta
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Pezzotti, F.; Therisod, M.
Enantioselective oxidation of thioanisole with an alcohol oxidase/peroxidase bienzymatic system
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The regulation of peroxisomal matrix enzymes (alcohol oxidase and catalase) formation by the product of the gene Mth1 in methylotrophic yeast Pichia methanolica
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Immobilization of Hansenula polymorpha alcohol oxidase for alcohol biosensor applications
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Dissociation and reconstitution studies of a broad substrate specific multimeric alcohol oxidase protein produced by Aspergillus terreus
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Isobe, K.; Takahashi, T.; Ogawa, J.; Kataoka, M.; Shimizu, S.
Production and characterization of alcohol oxidase from Penicillium purpurescens AIU 063
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Penicillium purpurescens, Penicillium purpurescens AIU 063
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Zhang, A.L.; Luo, J.X.; Zhang, T.Y.; Pan, Y.W.; Tan, Y.H.; Fu, C.Y.; Tu, F.Z.
Recent advances on the GAP promoter derived expression system of Pichia pastoris
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Komagataella pastoris
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Gvozdev, A.R.; Tukhvatullin, I.A.; Gvozdev, R.I.
Purification and properties of alcohol oxidase from Pichia putida
Biochemistry (Moscow)
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Pichia putida
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Jadhav, U.; Dawkar, V.; Tamboli, D.; Govindwar, S.
Purification and characterization of veratryl alcohol oxidase from Comamonas sp. UVS and its role in decolorization of textile dyes
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Comamonas sp., Comamonas sp. UVS
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Goswami, P.; Chinnadayyala, S.S.; Chakraborty, M.; Kumar, A.K.; Kakoti, A.
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Kim, Y.; Rykov, V.; Ashin, V.; Molochkov, N.; Skarga, Y.
Thermodynamic behavior and conformational changes of alcohol oxidase from yeast Hansenula polymorpha
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Ogataea angusta, Ogataea angusta NCYC 495
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Liu, Y.; Pan, J.; Wei, P.; Zhu, J.; Huang, L.; Cai, J.; Xu, Z.
Efficient expression and purification of recombinant alcohol oxidase in Pichia pastoris
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Komagataella pastoris, Komagataella pastoris GS115
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Kjellander, M.; Goetz, K.; Liljeruhm, J.; Boman, M.; Johansson, G.
Steady-state generation of hydrogen peroxide: kinetics and stability of alcohol oxidase immobilized on nanoporous alumina
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Komagataella pastoris
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Linke, D.; Lehnert, N.; Nimtz, M.; Berger, R.G.
An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity
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Phanerodontia chrysosporium, Phanerodontia chrysosporium (T2M2J4), Phanerodontia chrysosporium DSMZ 1547
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Pickl, M.; Fuchs, M.; Glueck, S.M.; Faber, K.
The substrate tolerance of alcohol oxidases
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Komagataella pastoris
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Virk, S.; Baruah, V.; Goswami, P.
Giant vesicles as encapsulating matrix for stabilizing alcohol oxidase and as container for coupled enzymatic reactions
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Aspergillus terreus, Aspergillus terreus MTCC 6324
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Das, M.; Barbora, L.; Das, P.; Goswami, P.
Biofuel cell for generating power from methanol substrate using alcohol oxidase bioanode and air-breathed laccase biocathode
Biosens. Bioelectron.
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Komagataella pastoris
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Chinnadayyala, S.R.; Santhosh, M.; Singh, N.K.; Goswami, P.
Alcohol oxidase protein mediated in-situ synthesized and stabilized gold nanoparticles for developing amperometric alcohol biosensor
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Komagataella pastoris
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Zhao, L.; Liu, Q.; Yan, S.; Chen, Z.; Chen, J.; Li, X.
Multimeric immobilization of alcohol oxidase on electrospun fibers for valid tests of alcoholic saliva
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Komagataella pastoris
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Yamada, M.; Higashiyama, T.; Kishino, S.; Kataoka, M.; Ogawa, J.; Shimizu, S.; Isobe, K.
Novel alcohol oxidase with glycolate oxidase activity from Ochrobactrum sp. AIU 033
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Ochrobactrum sp.
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Koch, C.; Neumann, P.; Valerius, O.; Feussner, I.; Ficner, R.
Crystal structure of alcohol oxidase from Pichia pastoris
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Komagataella pastoris (P04842), Komagataella pastoris, Komagataella pastoris X33 (P04842)
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Vonck, J.; Parcej, D.N.; Mills, D.J.
Structure of alcohol oxidase from Pichia pastoris by cryo-electron microscopy
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Ribeaucourt, D.; Bissaro, B.; Guallar, V.; Yemloul, M.; Haon, M.; Grisel, S.; Alphand, V.; Brumer, H.; Lambert, F.; Berrin, J.; Lafond, M.
Comprehensive insights into the production of long chain aliphatic aldehydes using a copper-radical alcohol oxidase as biocatalyst
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2021
Colletotrichum graminicola (E3QHV8)
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Martin, C.; Trajkovic, M.; Fraaije, M.W.
Production of hydroxy acids selective double oxidation of diols by flavoprotein alcohol oxidase
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Phanerodontia chrysosporium (T2M2J4), Phanerodontia chrysosporium
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Tjallinks, G.; Martin, C.; Fraaije, M.
Enantioselective oxidation of secondary alcohols by the flavoprotein alcohol oxidase from Phanerochaete chrysosporium
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Phanerodontia chrysosporium (T2M2J4), Phanerodontia chrysosporium
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Nguyen, Q.T.; Romero, E.; Dijkman, W.P.; de Vasconcellos, S.P.; Binda, C.; Mattevi, A.; Fraaije, M.W.
Structure-based engineering of Phanerochaete chrysosporium alcohol oxidase for enhanced oxidative power toward glycerol
Biochemistry
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Phanerodontia chrysosporium (T2M2J4), Phanerodontia chrysosporium
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Semenova, D.; Pinto, T.; Koch, M.; Gernaey, K.V.; Junicke, H.
Electrochemical tuning of alcohol oxidase and dehydrogenase catalysis via biosensing towards butanol-1 detection in fermentation media
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Komagataella pastoris
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Cajnko, M.; Novak, U.; Grilc, M.; Likozar, B.
Enzymatic conversion reactions of 5-hydroxymethylfurfural (HMF) to bio-based 2,5-diformylfuran (DFF) and 2,5-furandicarboxylic acid (FDCA) with air Mechanisms, pathways and synthesis selectivity
Biotechnol. Biofuels
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Komagataella phaffii (P04842), Komagataella phaffii GS115 (P04842)
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Portela, R.M.C.; Vogl, T.; Ebner, K.; Oliveira, R.; Glieder, A.
Pichia pastoris alcohol oxidase 1 (AOX1) core promoter engineering by high resolution systematic mutagenesis
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Komagataella phaffii (F2QY27), Komagataella phaffii, Komagataella phaffii ATCC 76273 (F2QY27)
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Heath, R.S.; Birmingham, W.R.; Thompson, M.P.; Taglieber, A.; Daviet, L.; Turner, N.J.
An engineered alcohol oxidase for the oxidation of primary alcohols
ChemBioChem
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2019
Arthrobacter globiformis (Q7X2H8)
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Aalbers, F.S.; Fraaije, M.W.
Design of artificial alcohol oxidases alcohol dehydrogenase-NADPH oxidase fusions for continuous oxidations
ChemBioChem
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Thermoanaerobacter brockii, Levilactobacillus brevis
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Ruff, A.; Pinyou, P.; Nolten, M.; Conzuelo, F.; Schuhmann, W.
A self-powered ethanol biosensor
ChemElectroChem
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Komagataella phaffii
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Yang, D.; Reyes-De-Corcuera, J.
Increased activity of alcohol oxidase at high hydrostatic pressure
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Komagataella phaffii
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Takahashi, F.; Igarashi, K.; Takimura, Y.; Yamamoto, T.
Elucidation of secondary alcohol metabolism in Starmerella bombicola and contribution of primary alcohol oxidase FAO1
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Mangkorn, N.; Kanokratana, P.; Roongsawang, N.; Laobuthee, A.; Laosiripojana, N.; Champreda, V.
Synthesis and characterization of Ogataea thermomethanolica alcohol oxidase immobilized on barium ferrite magnetic microparticles
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Ogataea thermomethanolica (nom. inval.) (A0A067YIW8), Ogataea thermomethanolica (nom. inval.)
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Matsumura, K.; Yamada, M.; Yamashita, T.; Muto, H.; Nishiyama, K.I.; Shimoi, H.; Isobe, K.
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Komagataella phaffii
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Khan, M.W.; Murali, A.
Modeling of alcohol oxidase enzyme of Candida boidinii and in silico analysis of competitive binding of proton ionophores and FAD with enzyme
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Mangkorn, N.; Kanokratana, P.; Roongsawang, N.; Laosiripojana, N.; Champreda, V.
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Ogataea thermomethanolica (nom. inval.) (A0A067YIW8), Ogataea thermomethanolica (nom. inval.)
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