BRENDA home
History
Information on EC 1.1.3.13 - alcohol oxidase
for references in articles please use BRENDA:EC1.1.3.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.3.13 alcohol oxidaseIUBMB Comments
The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor [1,3]. The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism . The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.
Specify your search results
Word Map
- 1.1.3.13
- pichia
- pastoris
-
methylotrophic
- polymorpha
- hansenula
- formaldehyde
- catalase
-
biosensors
-
electrode
- candida
-
methanol-inducible
- oxidases
-
amperometric
- boidinii
- alpha-factor
- analysis
- methanolica
-
flavoenzyme
-
octameric
-
vanillyl
-
methanol-grown
- dihydroxyacetone
-
methanol-utilizing
-
isoamyl
-
coniferyl
-
zeocin
- komagataella
-
screen-printed
-
ogataea
- simplicissimum
-
alpha-mating
- synthesis
- molecular biology
-
peroxisome-deficient
- degradation
- microbodies
-
ppic9k
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
alcohol oxidase 1, alcohol oxidase 2, alcohol oxidase A, alcohol oxidase B, alcohol oxidase I, alcohol: O2 oxidoreductase, alcohol:dioxygen-oxidoreductase, alcohol:O2 oxidoreductase, AlcOx, AOd, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AOd
AOext
AOint
AOX
AOX1
ethanol oxidase
extracellular alcohol oxidase
FAD-dependent alcohol oxidase
intracellular alcohol oxidase
methanol oxidase
oxidase, alcohol
-
-
-
-
P-AOD
primary alcohol oxidase
SCAO
short chain alcohol oxidase
VAO
veratryl alcohol oxidase
AOX
-
-
ethanol oxidase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + O2 = an aldehyde + H2O2
ping-pong mechanism operates via a two-electron transfer from substrate to oxygen
-
a primary alcohol + O2 = an aldehyde + H2O2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
alcohol:oxygen oxidoreductase
The enzymes from the fungi Candida methanosorbosa and several Basidiomycetes species contain an FAD cofactor [1,3]. The enzyme from the phytopathogenic fungi Colletotrichum graminicola and Colletotrichum gloeosporioides utilize a mononuclear copper-radical mechanism [4]. The enzyme acts on primary alcohols and unsaturated alcohols, and has much lower activity with branched-chain and secondary alcohols.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9073-63-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
butanaldehyde + H2O2
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
1-pentanol + O2
pentanaldehyde + H2O2
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
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-methoxyethanol + O2
2-methoxyethanal + H2O2
-
40% of the activity with methanol
-
-
?
2-methyl-1-butanol + O2
2-methyl-1-butanal + H2O2
-
22% of the activity with methanol
-
-
?
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
-
-
?
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
-
-
?
4-chloro-1-butanol + O2
4-chloro-1-butanal + H2O2
-
11% of the activity with methanol
-
-
?
arabitol + O2
?
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
formaldehyde + p-benzoquinone
formic acid + p-benzoquinol
-
p-benzoquinone, having the highest redox potential, proves to be the most efficient artificial electron acceptor
-
-
?
prop-2-en-1-ol + O2
acrylaldehyde + H2O2
-
81% of the activity with methanol
-
-
?
propylene glycol + O2
?
-
low activity with intra- and extracellular enzymes
-
-
?
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
54% of the activity with methanol
-
-
?
1-octanol + O2
n-octanal + H2O2
-
2.4% 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
-
33.5% of the activity with methanol
-
-
?
1-pentanol + O2
n-pentanal + H2O2
[Candida] methanosorbosa M-2003
-
33.5% 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
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
-
-
?
2-butanol + O2
2-butanone + H2O2
-
3.5% of the activity with methanol
-
-
?
2-butanol + O2
2-butanone + H2O2
[Candida] methanosorbosa M-2003
-
3.5% of the activity with methanol
-
-
?
2-mercaptoethanol + O2
2-mercaptoethanal + H2O2
-
25% of the activity with methanol
-
-
?
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-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
?
allylalcohol + O2
acrolein + H2O2
93% of the activity with methanol
-
-
?
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
[Candida] methanosorbosa M-2003
-
21.3% of the activity with methanol
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
6% of the activity with methanol
-
-
?
chloroethanol + O2
chloroethanal + H2O2
-
2-chloroethanol, 70% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
very low activity in cells grown on n-hexadecane
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
28% of the activity with methanol
-
?
ethanol + O2
acetaldehyde + H2O2
-
106% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
106% 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
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
-
82% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
10% activity compared to glycolate
-
-
?
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
-
intra- and extracellular enzymes
-
-
?
ethanol + O2
acetaldehyde + H2O2
-
97.8% of the activity with methanol
-
-
?
ethanol + O2
acetaldehyde + H2O2
[Candida] methanosorbosa M-2003
-
97.8% of the activity with methanol
-
-
?
ethylene glycol + O2
?
-
12% 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 mono-methylether + O2
methoxyacetaldehyde + H2O2
-
10% of the activity with methanol
-
-
?
formaldehyde + O2
formate + H2O2
-
23% of the activity with methanol
-
?
formaldehyde + O2
formic acid + H2O2
-
28% of the activity with methanol
-
-
?
formaldehyde + O2
formic acid + H2O2
-
28% of the activity with methanol
-
-
?
glycerol + O2
glyceraldehyde + H2O2
17% activity compared to methanol
-
-
?
glycerol + O2
glyceraldehyde + H2O2
-
17% activity compared to methanol
-
-
?
isobutanol + O2
isobutanal + H2O2
-
21% of the activity with methanol
-
-
?
isobutanol + O2
isobutyraldehyde + H2O2
-
1.2% of the activity with methanol
-
-
?
isopropanol + O2
2-propanone + H2O2
-
21% of the activity with methanol
-
-
?
isopropanol + O2
2-propanone + H2O2
-
6.9% of the activity with methanol
-
-
?
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
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
-
enzyme expression is tightly regulated, three regulatory sequences are involved
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
100% activity
-
-
?
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
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
methanol + O2
formaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
n-butanol + O2
butanal + H2O2
-
67% of the activity with methanol
-
-
?
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
-
20% 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
-
52.2% of the activity with methanol
-
-
?
n-heptanol + O2
n-heptanal + H2O2
-
substrates with highest affinity
-
-
?
n-hexanol + O2
n-hexanal + H2O2
-
6.3% of the activity with methanol
-
-
?
n-pentanol + O2
n-pentanal + H2O2
13% activity compared to methanol
-
-
?
n-pentanol + O2
n-pentanal + H2O2
-
13% 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
-
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
-
43% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
43% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
72.2% of the activity with methanol
-
-
?
n-propanol + O2
n-propanal + H2O2
-
77.5% of the activity with methanol
-
-
?
n-propanol + O2
propionaldehyde + H2O2
-
intra- and extracellular enzymes
-
-
?
propargyl alcohol + O2
propargyl aldehyde + H2O2
-
90% of the activity with methanol
-
-
?
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
?
-
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
?
-
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
?
-
-
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
-
-
?
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ethanol + O2
acetaldehyde + H2O2
-
very low activity in cells grown on n-hexadecane
-
-
?
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
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
-
enzyme expression is tightly regulated, three regulatory sequences are involved
-
-
?
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
-
key enzyme of methanol metabolism
-
-
?
methanol + O2
formaldehyde + H2O2
-
key enzyme of methanol metabolism
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
5 oxygen-stable red flavin semiquinones (ESR-spectroscopy) plus 2 oxidized flavins per octamer, the reconstituted enzyme which lacks the flavin semiquinones is still half as active as the native enzyme
FAD
-
one prosthetic group per subunit, a flavoprotein, binding structure, fine tuning of the enzyme activity may be regulated via modifications of the cofactor FAD, one of these mechanisms involves the autoconversion of the naturally occurring FAD moiety to the modified form, i.e. mFAD or a-FAD
FAD
-
one prosthetic group per subunit, a flavoprotein, fine tuning of the enzyme activity may be regulated via modifications of the cofactor FAD, one of these mechanisms involves the autoconversion of the naturally occurring FAD moiety to the modified form, i.e. mFAD or a-FAD
FAD
-
flavin is non-covalently but avidly associated. Peptide mass fingerprinting studies show the presence of two FAD binding domains in 63 kDa protein
FAD
-
noncovalently bound to the adenine moiety to the N-terminal domain of the subunit in the active site of the enzyme
flavin
-
noncovalently bound flavin different from FAD, FMN, and riboflavin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe3+
-
the enzyme contains 2 iron atoms and shows 112% activity at 1 mM Fe3+
MgCl2
-
1 mM, increases the enzyme activity to nearly 50% for both short chain-, and long chain alcohol substrates
additional information
additional information
-
the enzyme is not influenced by Mn2+, Co2+, Ni2+, and Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KBr
-
3.5 M at 30°C for 1-2 h: partial inactivation, KBr + urea: complete inactivation
p-chloromercuribenzoate
Pichia putida
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
Urea
-
6 M, at 30°C for 1-2 h: partial inactivation, urea + KBr: complete inactivation
5,5'-dithiobis(2-nitrobenzoate)
Pichia putida
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
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
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
iodoacetate
-
time-dependent inactivation, reversible on removal of excess inhibitor
PCMB
-
t1/2: 11 min, beta-mercaptoacetic acid restores activity, substrates or products slow the inactivation rate
additional information
-
no inhibition by ethylene glycol, even at high concentrations
-
additional information
-
glycerol represses enzyme expression, the enzyme expression is derepressed under glycerol limitations, growth on both methanol and glycerol are not repressed
-
additional information
-
2-propin-1-ol and methylenecyclopropyl alcohol are not suicide substrates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferrocene
-
1 mM, increases the alcohol oxidase activity only for the short chain alcohol substrate to 47% of the original activity
gold nanoparticle
-
the catalytic efficiency of gold nanoparticle-conjugated enzyme is increased by 18% from the free enzyme
-
additional information
-
methanol induces the enzyme irrespective of the presence of glycerol
-
additional information
-
induced by carbon starvation and during later stages of infection, deletion results in reduced pathogenicity
-
additional information
-
induced under conditions of penicillin production
-
additional information
-
the enzyme is activated 2fold by incubation at pH 6.0 and 40°C for 60 min, whereas the Km values for ethanol and ethylene glycol do not change
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hepatitis B
Expression of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris using the GAP promoter.
Hepatitis B
Simple high-cell density fed-batch technique for high-level recombinant protein production with Pichia pastoris: Application to intracellular production of Hepatitis B surface antigen.
Hepatitis B
Simultaneous expression of the S and L surface antigens of hepatitis B, and formation of mixed particles in the methylotrophic yeast, Hansenula polymorpha.
Influenza, Human
Expression of functional influenza virus RNA polymerase in the methylotrophic yeast Pichia pastoris.
Influenza, Human
Protection of mice against a lethal influenza challenge by immunization with yeast-derived recombinant influenza neuraminidase.
Neoplasms
High level expression of heterologous proteins in methylotrophic yeast Pichia pastoris.
Neoplasms
High-level expression, purification, and characterization of recombinant human tumor necrosis factor synthesized in the methylotrophic yeast Pichia pastoris.
Phytoplasma Disease
A potential role for an extracellular methanol oxidase secreted by Moniliophthora perniciosa in Witches' broom disease in cacao.
Zellweger Syndrome
Transport of microinjected alcohol oxidase from Pichia pastoris into vesicles in mammalian cells: involvement of the peroxisomal targeting signal.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0407
-
cell-free extract, with glycolate as substrate, at pH 5.5 and 30°C
183
-
native intermediate dissociated enzyme protein, substrate phenyl-3-propanol
190
-
native intermediate dissociated enzyme protein, substrate n-heptanol
3.44
37
-
native intermediate dissociated enzyme protein, substrate (R)-2-octanol
4.02
-
after 101fold purification, with glycolate as substrate, at pH 5.5 and 30°C
49
-
native intermediate dissociated enzyme protein, substrate n-dodecanol
additional information
additional information
-
substrate specificity of native, intermediate dissociated protein, and re-associated protein, overview. The re-associated enzyme protein shows poor activity with substrate (R)-2-octanol
additional information
-
the specific activity of the crude enzyme and after 13.9fold purification is 0.064 and 0.89 units/mg, respectively, using veratryl alcohol as substrate at pH 3.0 and 65°C. The substrate specificity of the VAO enzyme is 1.64 units/mg for n-propanol, 1.43 units/mg for veratryl alcohol, 0.48 units/mg for ethanol, 0.36 units/mg for L-dopa, 0.34 units/mg for indole and hydroxyquinone, 0.28 units/mg for L-tryptophan, and 0.03 units/mg for xylidine. One unit of an enzyme activity is defined as a change in absorbance unit/min/mg protein
additional information
-
development of Prussian blue-based amperometric sensor measuring H2O2 concentration as a tool for the study of Pichia pastoris alcohol oxidase-catalyzed reactionsPrussian blue-based amperometric sensor as a tool for the study of alcohol oxidase-catalyzed reactions, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM