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(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
-
180% activity compared to glycolate
-
-
?
1-hexanol + O2
hexanal + H2O2
-
300% activity compared to glycolate
-
-
?
1-octanol + O2
n-octanal + H2O2
1-octanol + O2
octanal + H2O2
-
189% activity compared to glycolate
-
-
?
1-pentanol + O2
n-pentanal + H2O2
1-pentanol + O2
pentanal + H2O2
-
448% activity compared to glycolate
-
-
?
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-undecanol + O2
undecanal + 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
A8DPS4
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
A8DPS4
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
chloroethanol + O2
chloroethanal + H2O2
crotyl alcohol + O2
(2E)-but-2-enal + H2O2
-
-
-
-
?
D-ribose + O2
? + H2O2
-
-
-
-
?
decanol + O2
decanal + 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
hexadecanol + O2
hexadecanal + 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
acetaldehyde + H2O2
-
-
-
-
?
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
pentan-1-ol + O2
pentanal + H2O2
-
50% of the activity with methanol
-
-
?
pentan-2-ol + O2
pentanone + H2O2
-
56% of the activity with methanol
-
-
?
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
-
-
-
-
?
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
-
373% activity compared to glycolate
-
-
?
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
A8DPS4
54% of the activity with methanol
-
-
?
1-octanol + O2

n-octanal + H2O2
-
2.4% of the activity with methanol
-
-
?
1-octanol + O2
n-octanal + H2O2
-
-
-
-
-
1-pentanol + O2

n-pentanal + H2O2
-
1% 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
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
A8DPS4
22% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
-
30% of the activity with methanol
-
-
?
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
A8DPS4
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
-
63% activity compared to glycolate
-
-
?
1-propanol + O2
propanal + H2O2
-
63% activity compared to glycolate
-
-
?
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
-
-
-
-
?
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-propyn-1-ol + O2

propyn-1-al + H2O2
-
45% of the activity with methanol
-
-
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
-
oxidized to mechanism-based irreversible inactivator: propynal
mechanism-based inhibitor
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
Poria contigua
-
-
-
-
?
3-phenylpropan-1-ol + O2

3-phenylpropanal + H2O2
-
-
-
-
?
3-phenylpropan-1-ol + O2
3-phenylpropanal + H2O2
-
-
-
-
?
allylalcohol + O2

acrolein + H2O2
A8DPS4
93% of the activity with methanol
-
-
?
allylalcohol + O2
acrolein + H2O2
-
-
-
-
-
allylalcohol + O2
acrolein + H2O2
-
-
-
-
?
benzyl alcohol + O2

benzaldehyde + H2O2
-
21.3% of the activity with methanol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
-
21.3% of the activity with methanol
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
A8DPS4
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
-
-
?
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
-
-
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
2-chloroethanol, 70% 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
-
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
-
106% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
106% of the activity with methanol
-
-
?
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
-
-
?
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
A8DPS4
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
-
10% activity compared to glycolate
-
-
?
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
-
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
-
-
?
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
-
-
-
?
formaldehyde + O2
formate + 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

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
-
-
-
-
?
formaldehyde + O2
formic acid + H2O2
-
low activity
-
-
?
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
-
-
?
glycolate + O2

glyoxylate + H2O2
-
100% activity
-
-
?
glycolate + O2
glyoxylate + H2O2
-
100% activity
-
-
?
hexadecanol + O2

hexadecanal + H2O2
-
62% of the activity with methanol
-
-
?
hexadecanol + O2
hexadecanal + H2O2
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
best substrate
-
-
?
methanol + O2
formaldehyde + H2O2
A8DPS4
-
-
-
?
methanol + O2
formaldehyde + H2O2
A8DPS4
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
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
-
-
?
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
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
-
52.2% 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-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
-
6.3% of the activity with methanol
-
-
?
n-hexanol + O2
n-hexanal + H2O2
-
-
-
-
?
n-hexanol + O2
n-hexanal + H2O2
-
4% 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
-
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
-
77.5% 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
-
-
-
-
?
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

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
?
-
-
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
-
-
-
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
?
-
-
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
?
-
A5LGE7
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
?
-
-
the enzyme does not oxidize benzyl alcohol, glycolaldehyde, glyoxylate, ethylene glycol, glycerol, or methanol
-
-
-
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
?
-
A5LGE9
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
?
-
Q9UVU1
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
?
-
A5LGF2
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
-
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
-
-
-
-
?
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
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
A8DPS4
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
-
-
-
-
?
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
-
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
-
-
-
-
?
additional information

?
-
-
the enzyme is the key enzyme of methanol metabolism in methylotrophic yeast species, overview
-
-
-
additional information
?
-
Q00922
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
?
-
Q5S057
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
?
-
Q5S058
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
?
-
A5LGE3
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
?
-
A5LGE4
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
?
-
A5LGE5
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
?
-
A5LGD9
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
?
-
A5LGE0
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
?
-
A5LGE6
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
?
-
-
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
?
-
F2QY27
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
?
-
F2R038
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
?
-
A5LGE7
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
?
-
P04841
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
?
-
A5LGE9
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
?
-
A5LGF0
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
?
-
Q9UVU1
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
?
-
Q9UVU2
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
?
-
A5LGF1
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
?
-
A5LGF2
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
?
-
A5LGF3
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
?
-
A5LGE1
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
?
-
A5LGE2
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
?
-
A5LGF4
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
?
-
A5LGE8
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
?
-
Q5S059
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
?
-
Q5S060
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.
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1,12-dichlorododecane
-
-
2,2'-dipyridyl
-
1 mM, 13% inhibition
2-Aminoethanol
-
1 mM, 70% inhibition
3-Pentanol
-
1 mM, 16% inhibition
4-chloromercuribenzoate
-
0.1 mM, 31% inhibition
5,5'-dithiobis(2-nitrobenzoate)
5,5'-dithiobis-(2-nitrobenzoic acid)
-
-
8-hydroxyquinoline
-
1 mM, 6% inhibition
AgNO3
-
1 mM, complete loss of activity
dithiothreitol
-
85% residual activity at 0.5 mM
DMSO
-
complete inhibition by 50% DMSO
Fe2+
-
slight inhibition of extracellular enzyme
HgCl2
-
1 mM, 44% inhibition
imidazole
-
1 mM, 20% inhibition
iodoacetic acid
-
59% residual activity at 1 mM
KBr
-
3.5 M at 30°C for 1-2 h: partial inactivation, KBr + urea: complete inactivation
L-cysteine
-
70% residual activity at 0.5 mM
Mercuric acetate
-
0.1 mM, complete inhibition
Mercuric chloride
-
1 mM, complete inhibition
Metal chelators
-
slight
-
methanol
-
substrate inhibition
Mo6+
-
1 mM, 94% inhibition
Monoiodoacetic acid
-
1 mM, 31% inhibition
N-ethylmaleimide
-
84% residual activity at 1 mM
Na+
-
slight inhibition of extracellular enzyme
o-phenanthroline
-
93% residual activity at 1 mM
p-chloromercuribenzoate
Pichia putida
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
p-chloromercuribenzoic acid
-
-
p-hydroxymercuribenzoate
-
1 mM, complete inhibition
propargyl alcohol
-
irreversible
Semicarbazide
-
91% residual activity at 1 mM
Tetraethylthiuram disulfide
-
5 mM, more than 70% loss of activity
Thiosemicarbazide
-
1 mM, 31% loss of activity
Urea
-
6 M, at 30°C for 1-2 h: partial inactivation, urea + KBr: complete inactivation
Zn2+
-
35% residual activity at 0.5 mM
1,10-phenanthroline

-
1 mM, 56% loss of activity
1,10-phenanthroline
-
1 mM, 10% inhibition
1,4-butynediol

-
-
1,4-butynediol
-
irreversible
4-Hydroxy-2-butynal

-
irreversible
5,5'-dithiobis(2-nitrobenzoate)

Pichia putida
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
5,5'-dithiobis(2-nitrobenzoate)
-
1 mM, 35% inhibition
acetamide

-
-
acetamide
-
1 mM, 10% inhibition
Ag+

-
-
Cd2+

-
1 mM, 48% inhibition
Cd2+
-
65% residual activity at 0.5 mM
Cu2+

-
1 mM, 95% inhibition
Cu2+
-
reversible by EDTA
Cu2+
-
1 mM CuSO4, 30 min, strong
Cu2+
-
1 mM, 86% inhibition
Cu2+
-
15% residual activity at 0.5 mM
Cu2+
-
91% residual activity at 1 mM
Cu2+
-
1 mM CuCl2, complete inhibition
Cu2+
-
1 mM CuSO4, 50% inhibition
Cyclopropanone

-
0.05 mM, pH 7.5, 20°C, pseudo-first order loss of enzymatic activity, t1/2: 39 min, no reversal by removal of the inhibitor, rate of inactivation is reduced in the presence of substrate, product, or glutathione, inactivation is completely prevented by reduction of the FAD coenzyme prior to addition of the inactivator
Cyclopropanone
-
suicide substrate
diethyldicarbonate

-
-
EDTA

-
75% residual activity at 0.5 mM
EDTA
-
91% residual activity at 1 mM
EDTA
-
slight inhibition of intra- and extracellular enzymes
FeSO4

-
-
FeSO4
-
1 mM, complete inhibition
formaldehyde

-
-
H2O2

-
methanol or catalase partially protects
H2O2
-
inhibits at 5 mM, at 7.8 mM the enzyme maintains 50% of its initial activity after 0.5 h of incubation at 4°C
Hg2+

-
reversible by mercaptoethanol
Hg2+
-
1 mM HgCl2, 30 min, strong
Hg2+
-
0.1 mM, complete inhibition
Hg2+
-
52% residual activity at 0.5 mM
Hg2+
-
strong inhibition of intra- and extracellular enzymes
hydrazine

-
1 mM, complete inhibition
hydrazine
-
89% residual activity at 1 mM
hydroquinone

-
1 mM, 30 min, strong
hydroxylamine

-
1 mM, complete inhibition
hydroxylamine
-
72% residual activity at 1 mM
hydroxylamine
-
1 mM, 21% inhibition
iodoacetate

-
time-dependent inactivation, reversible on removal of excess inhibitor
iodoacetate
-
1 mM, 38% inhibition
K+

-
75% residual activity at 0.5 mM
K+
-
slight inhibition of extracellular enzyme
KCN

-
1 mM 56% inhibition
KCN
-
93% residual activity at 1 mM
KCN
-
inhibition of intra- and extracellular enzymes
Mg2+

-
90% residual activity at 0.5 mM
Mg2+
-
93% residual activity at 1 mM
Mn2+

-
62% residual activity at 0.5 mM
Mn2+
-
slight inhibition of intra- and extracellular enzymes
NaN3

-
-
NaN3
-
competitive, reversible
NaN3
Poria contigua
-
strong
NaN3
-
inhibition of intra- and extracellular enzymes
NEM

-
1 mM, 30 min, strong
NEM
-
1 mM, 10% inhibition
NEM
-
slight inhibition of intra- and extracellular enzymes
NiCl2

-
-
NiCl2
-
1 mM, complete inhibition
PCMB

-
5 mM, complete loss of activity
PCMB
-
1 mM, complete inhibition
PCMB
-
t1/2: 11 min, beta-mercaptoacetic acid restores activity, substrates or products slow the inactivation rate
PCMB
-
1 mM, 30 min, strong
PCMB
-
0.1 mM; 39% inhibition
PCMB
Poria contigua
-
1 mM, complete inhibition
phenylhydrazine

-
1 mM, complete inhibition
phenylhydrazine
-
1 mM, complete inhibition
phenylhydrazine
-
1% residual activity at 1 mM
Propynal

-
-
Sodium acetate

-
-
Sodium azide

-
the enzyme is completely inhibited by 0.5 mM sodium azide
Sodium azide
-
97% residual activity at 1 mM
Sodium azide
-
1 mM, 15% inhibition
additional information

-
no inhibition by ethylene glycol, even at high concentrations
-
additional information
-
2-propin-1-ol and methylenecyclopropyl alcohol are not suicide substrates
-
additional information
-
not inhibited by Ba2+, Ca2+, and Na+
-
additional information
-
glycerol represses enzyme expression, the enzyme expression is derepressed under glycerol limitations, growth on both methanol and glycerol are not repressed
-
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