Information on EC 1.1.3.13 - alcohol oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.3.13
-
RECOMMENDED NAME
GeneOntology No.
alcohol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + O2 = an aldehyde + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Methane metabolism
-
-
methanol oxidation to formaldehyde IV
-
-
Microbial metabolism in diverse environments
-
-
methane metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-63-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MTCC 6324
-
-
Manually annotated by BRENDA team
strain B191039
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
isolated in Thailand
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
strain 25-A
-
-
Manually annotated by BRENDA team
strain 25-A
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
gene faot
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
indigenous, filamentous fungus isolated from petroleum-contaminated soils,growth on decane or hexadecane, two isoforms
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Hansenula sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain IFP 206
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
strain DL-1
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment; var. minuta
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
gene AOX1
-
-
Manually annotated by BRENDA team
isolated in Thailand
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
strain RI017 was isolated as a formaldehyde-resistant fungus from wastewater containing formaldehyde
-
-
Manually annotated by BRENDA team
strain RI017 was isolated as a formaldehyde-resistant fungus from wastewater containing formaldehyde
-
-
Manually annotated by BRENDA team
gene AOX1
-
-
Manually annotated by BRENDA team
gene AOX
-
-
Manually annotated by BRENDA team
strain AIU 063
-
-
Manually annotated by BRENDA team
strain AIU 063
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
Pichia putida
-
-
-
Manually annotated by BRENDA team
Polyporus obtusus
-
-
-
Manually annotated by BRENDA team
Poria contigua
-
-
-
Manually annotated by BRENDA team
strain NBRC 31693, a thermophilic fungus
-
-
Manually annotated by BRENDA team
strain NBRC 31693, a thermophilic fungus
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the peroxisomal enzyme alcohol oxidase plays key role in methanol dissimilation in yeast
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-octanol + O2
2-octanone + H2O2
show the reaction diagram
-
-
-
-
?
(R)-2-octanol + O2
octan-2-one + H2O2
show the reaction diagram
1,2-propanediol + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
1,3-butylene glycol + O2
? + H2O2
show the reaction diagram
1,4-butynediol + O2
4-hydroxy-2-butyn-1-al + H2O2
show the reaction diagram
-
oxidized to mechanism-based irreversible inactivator: 4-hydroxy-2-butynal
mechanism-based inhibitor
?
1-butanol + O2
butanaldehyde + H2O2
show the reaction diagram
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
1-butanol + O2
n-butanal + H2O2
show the reaction diagram
1-octanol + O2
n-octanal + H2O2
show the reaction diagram
1-pentanol + O2
n-pentanal + H2O2
show the reaction diagram
1-pentanol + O2
pentanaldehyde + H2O2
show the reaction diagram
-
intra- and extracellular enzymes, low activity with the intracellular enzyme
-
-
?
1-propanol + O2
n-propanal + H2O2
show the reaction diagram
2-butanol + O2
2-butanone + H2O2
show the reaction diagram
2-buten-1-ol + O2
2-buten-1-al + H2O2
show the reaction diagram
-
-
-
-
?
2-chloroethanol + O2
2-chloroethanal + H2O2
show the reaction diagram
-
66% of the activity with methanol
-
-
?
2-cyanoethanol + O2
2-cyanoethanal + H2O2
show the reaction diagram
-
30% of the activity with methanol
-
-
?
2-mercaptoethanol + O2
2-mercaptoethanal + H2O2
show the reaction diagram
2-methoxyethanol + O2
2-methoxyethanal + H2O2
show the reaction diagram
-
40% of the activity with methanol
-
-
?
2-methyl-1-butanol + O2
2-methyl-1-butanal + H2O2
show the reaction diagram
-
22% of the activity with methanol
-
-
?
2-methyl-1-propanol + O2
butan-2-one + H2O2
show the reaction diagram
7% of the activity with methanol
-
-
?
2-methyl-2-propanol + O2
?
show the reaction diagram
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
2-propanol + O2
2-oxopropane + H2O2
show the reaction diagram
-
-
-
-
?
2-propanol + O2
acetone + H2O2
show the reaction diagram
2-propen-1-ol + O2
2-propen-1-al + H2O2
show the reaction diagram
2-propyn-1-ol + O2
2-propyn-1-al + H2O2
show the reaction diagram
Poria contigua
-
-
-
-
?
2-propyn-1-ol + O2
propyn-1-al + H2O2
show the reaction diagram
3-chloro-1-propanol + O2
3-chloro-1-propanal + H2O2
show the reaction diagram
-
22% of the activity with methanol
-
-
?
3-methyl-1-butanol + O2
3-methylbutanal + H2O2
show the reaction diagram
7% of the activity with methanol
-
-
?
3-phenylpropan-1-ol + O2
3-phenylpropanal + H2O2
show the reaction diagram
4-chloro-1-butanol + O2
4-chloro-1-butanal + H2O2
show the reaction diagram
-
11% of the activity with methanol
-
-
?
4-hepten-1-ol + O2
4-hepten-1-al + H2O
show the reaction diagram
-
-
-
?
4-nonen-1-ol + O2
4-nonen-1-al + H2O2
show the reaction diagram
-
-
-
?
allylalcohol + O2
acrolein + H2O2
show the reaction diagram
arabitol + O2
?
show the reaction diagram
-
extracellular enzyme, no activity with the intracellular enzyme
-
-
?
benzyl alcohol + O2
benzaldehyde + H2O2
show the reaction diagram
bromoethanol + O2
bromoethanal + H2O2
show the reaction diagram
-
4% of the activity with methanol
-
-
?
chloroethanol + O2
chloroethanal + H2O2
show the reaction diagram
crotyl alcohol + O2
(2E)-but-2-enal + H2O2
show the reaction diagram
-
-
-
-
?
D-ribose + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
-
-
-
-
?
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
-
-
-
?
erythritol + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
ethanol + O2
acetaldehyde + H2O2
show the reaction diagram
ethylene glycol + O2
?
show the reaction diagram
ethylene glycol + O2
? + H2O2
show the reaction diagram
ethylene glycol mono-methylether + O2
methoxyacetaldehyde + H2O2
show the reaction diagram
formaldehyde + methylene blue
formic acid + ?
show the reaction diagram
-
-
-
-
?
formaldehyde + O2
formate + H2O2
show the reaction diagram
formaldehyde + O2
formic acid + H2O2
show the reaction diagram
formaldehyde + p-benzoquinone
formic acid + p-benzoquinol
show the reaction diagram
-
p-benzoquinone, having the highest redox potential, proves to be the most efficient artificial electron acceptor
-
-
?
formaldehyde + toluidine blue
formic acid + ?
show the reaction diagram
-
-
-
-
?
glucose + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
glycerol + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
hexanol + O2
hexanal + H2O2
show the reaction diagram
hydroxyquinone + O2
?
show the reaction diagram
-
-
-
-
?
indole + O2
?
show the reaction diagram
isoamyl alcohol + O2
3-methylbutanal + H2O2
show the reaction diagram
-
-
-
-
?
isoamyl alcohol + O2
? + H2O2
show the reaction diagram
-
2% of the activity with methanol
-
-
?
isobutanol + O2
isobutanal + H2O2
show the reaction diagram
isobutanol + O2
isobutyraldehyde + H2O2
show the reaction diagram
isopropanol + O2
2-propanone + H2O2
show the reaction diagram
L-DOPA + O2
?
show the reaction diagram
L-tryptophan + O2
?
show the reaction diagram
-
-
-
-
?
methanol + O2
formaldehyde + H2O2
show the reaction diagram
n-butanol + O2
butanal + H2O2
show the reaction diagram
n-butanol + O2
butanaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
n-butanol + O2
butyraldehyde + H2O2
show the reaction diagram
-
-
-
-
?
n-butanol + O2
n-butanal + H2O2
show the reaction diagram
n-dodecanol + O2
n-dodecanal + H2O2
show the reaction diagram
n-heptanol + O2
heptanaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
n-heptanol + O2
n-heptanal + H2O2
show the reaction diagram
n-hexanol + O2
n-hexanal + H2O2
show the reaction diagram
n-octanol + O2
octanaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
n-pentanol + O2
n-pentanal + H2O2
show the reaction diagram
n-propanol + O2
n-propanal + H2O2
show the reaction diagram
n-propanol + O2
propanal + H2O2
show the reaction diagram
-
-
-
-
?
n-propanol + O2
propanaldehyde + H2O2
show the reaction diagram
n-propanol + O2
propionaldehyde + H2O2
show the reaction diagram
pentan-1-ol + O2
pentanal + H2O2
show the reaction diagram
-
50% of the activity with methanol
-
-
?
pentan-2-ol + O2
pentanone + H2O2
show the reaction diagram
-
56% of the activity with methanol
-
-
?
phenyl-3-propanol + O2
3-phenylpropanal
show the reaction diagram
-
-
-
-
?
prop-2-en-1-ol + O2
acrylaldehyde + H2O2
show the reaction diagram
-
81% of the activity with methanol
-
-
?
propargyl alcohol + O2
propargyl aldehyde + H2O2
show the reaction diagram
propylene glycol + O2
?
show the reaction diagram
-
low activity with intra- and extracellular enzymes
-
-
?
ribitol + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
-
-
-
-
?
veratryl alcohol + O2
?
show the reaction diagram
xylidine + O2
?
show the reaction diagram
-
lowest specific activity with xylidine
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanol + O2
acetaldehyde + H2O2
show the reaction diagram
formaldehyde + O2
formic acid + H2O2
show the reaction diagram
-
-
-
-
?
isopropanol + O2
2-propanone + H2O2
show the reaction diagram
methanol + O2
formaldehyde + H2O2
show the reaction diagram
n-butanol + O2
butanaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
n-heptanol + O2
heptanaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
n-octanol + O2
octanaldehyde + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
slight activation of intracellular enzyme
MgCl2
-
1 mM, increases the enzyme activity to nearly 50% for both short chain-, and long chain alcohol substrates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,12-dichlorododecane
-
-
1,4-butynediol
2,2'-dipyridyl
-
1 mM, 13% inhibition
2-Aminoethanol
-
1 mM, 70% inhibition
2-mercaptoethanol
-
-
3-Pentanol
-
1 mM, 16% inhibition
4-chloromercuribenzoate
-
0.1 mM, 31% inhibition
4-Hydroxy-2-butynal
5,5'-dithiobis(2-nitrobenzoate)
8-hydroxyquinoline
-
1 mM, 6% inhibition
acetamide
-
1 mM, 10% inhibition
AgNO3
-
1 mM, complete loss of activity
Cyclopropanol
-
-
Cyclopropanone
diethyldicarbonate
-
-
dithiothreitol
-
85% residual activity at 0.5 mM
DMSO
-
complete inhibition by 50% DMSO
Fe2+
-
slight inhibition of extracellular enzyme
FeSO4
-
1 mM, complete inhibition
formaldehyde
-
-
HgCl2
-
1 mM, 44% inhibition
hydrazine
-
1 mM, complete inhibition
hydroquinone
-
1 mM, 30 min, strong
hydroxylamine
imidazole
-
1 mM, 20% inhibition
iodoacetate
KBr
-
3.5 M at 30C 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
Mg2+
-
90% residual activity at 0.5 mM
Mo6+
-
1 mM, 94% inhibition
Monoiodoacetic acid
-
1 mM, 31% inhibition
Na+
-
slight inhibition of extracellular enzyme
NiCl2
-
1 mM, complete inhibition
p-chloromercuribenzoate
Pichia putida
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
p-hydroxymercuribenzoate
-
1 mM, complete inhibition
phenylhydrazine
propargyl alcohol
-
irreversible
Propynal
Sodium acetate
-
-
Sodium azide
Tetraethylthiuram disulfide
-
5 mM, more than 70% loss of activity
Thiosemicarbazide
-
1 mM, 31% loss of activity
Urea
-
6 M, at 30C for 1-2 h: partial inactivation, urea + KBr: complete inactivation
Zn2+
-
35% residual activity at 0.5 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, 1.25fold activation
Ferrocene
-
1 mM, increases the alcohol oxidase activity only for the short chain alcohol substrate to 47% of the original activity
iodoacetamide
-
1 mM, 1.3fold activation
methanol
-
induces enzyme expression at 3%
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.3
(R)-2-octanol
-
-
36
1,4-butynediol
-
-
42.7
1-propanol
at pH 9.0 and 50C
27.2
2-mercaptoethanol
Poria contigua
-
-
261
2-propanol
-
pH 6.5, 22C, immobilized enzyme
3.2 - 10
2-propin-1-ol
0.18
4-hepten-1-ol
-
-
0.44
4-Hydroxy-2-butynal
-
-
0.42
4-nonen-1-ol
-
-
33.3
allyl alcohol
-
-
26.6
benzyl alcohol
-
-
0.075
butanol
-
-
71.5
D-ribose
-
-
0.018
Decanol
-
-
0.038
Dodecanol
-
-
670
erythritol
-
-
0.13 - 22.5
ethanol
0.95 - 9
ethylene glycol
1.59 - 10.5
formaldehyde
0.0005 - 0.023
hexadecanol
0.029
Hexanol
-
-
25
Isopropanol
Poria contigua
-
-
0.019 - 89.58
methanol
0.028 - 166
n-butanol
1.86
n-dodecanol
-
-
0.005 - 0.498
n-Heptanol
0.05
n-Octanol
-
pH 8.5, 30C, SCAO
10.9
n-Pentanol
at pH 9.0 and 50C
1.23 - 66
n-Propanol
0.34 - 1
O2
0.0032
Octanol
-
-
0.05
p-benzoquinone
-
-
2.3
phenyl-3-propanol
-
-
0.067
Propanol
-
-
250
ribitol
-
-
0.0056
Tetradecanol
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58
ethanol
Ogataea angusta
-
pH 7.5, 30C
32
formaldehyde
Ogataea angusta
-
pH 7.5, 30C
15.6 - 60
methanol
270
n-Heptanol
Aspergillus terreus
-
-
additional information
additional information
Candida boidinii
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00246
1,12-dichlorododecane
-
substrate: n-dodecanal
0.000014 - 0.00362
2-mercaptoethanol
0.42
4-Hydroxy-2-butynal
-
-
6500
methanol
-
-
0.02
Sodium azide
Poria contigua
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.21
-
free native enzyme, substrate n-propanol
0.33
-
immobilized native enzyme, substrate n-propanol
0.48
-
immobilized native enzyme, substrate crotyl alcohol
0.68
-
free native enzyme, substrate crotyl alcohol
1.62
-
substrate hexadecanol, pH 7.5, 25C
1.67
-
purified intracellular enzyme
1.86
-
substrate hexadecanol, pH 7.5, 25C
3.44
-
; purified enzyme
3.59
-
oxidation of ethanol
3.64
-
oxidation of ethylene glycol
6.6
-
-
6.68
-
immobilized native enzyme, substrate methanol
8.18
-
immobilized native enzyme, substrate ethanol
9.42
-
purified extracellular enzyme
9.48
-
free native enzyme, substrate methanol
10.23
-
free native enzyme, substrate ethanol
11.85
-
purified recombinant intracellular enzyme, pH 80, 25C
12.94
-
purified recombinant extracellular enzyme, pH 80, 25C
20.7
Poria contigua
-
-
23
-
purified enzyme
37
-
native intermediate dissociated enzyme protein, substrate (R)-2-octanol
42
-
re-associated enzyme protein, substrate n-dodecanol
45
-
re-associated enzyme protein, substrate phenyl-3-propanol
49
-
native intermediate dissociated enzyme protein, substrate n-dodecanol
62
-
native enzyme, substrate n-dodecanol
63
-
native enzyme, substrate (R)-2-octanol
96
-
re-associated enzyme protein, substrate n-heptanol
183
-
native intermediate dissociated enzyme protein, substrate phenyl-3-propanol
190
-
native intermediate dissociated enzyme protein, substrate n-heptanol
250
-
native enzyme, substrate phenyl-3-propanol
305
-
native enzyme, substrate n-heptanol
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
the free and immobilized enzyme show less than 45% of their maximum activities below pH 4.0 and approximately 85% at pH 10.0
5.5
16% of maximal activity
5.5 - 11
-
pH 5.5: 6% of maximal activity, pH 11.0: 12% of maximal activity
6 - 10
-
pH 6.0: about 65% of maximal activity, pH 10.0: 85% of maximal activity
6.5 - 8.3
-
about half-maximal activity at pH 6.5 and 8.3
6.7 - 9.8
-
about half-maximal activity at pH 6.7 and 9.8
7 - 10
more than 60% activity between pH 7.0 and 10.0
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25 - 30
-
thermoactivated enzyme
35 - 40
-
native, not thermoactivated enzyme
37.5
-
-
50 - 55
-
ethanol oxidation
additional information
-
the enzyme activity is enhanced to 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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18 - 45
-
half-maximal activity at 18C and 45C
20 - 45
-
activity range, 50% of maximal activity at 40C
30 - 80
-
activity range of the immobilized enzyme, 25% of maximal activity at 80C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
isoelectric focusing
5.9
-
purified intracellular enzyme
8.3 - 8.5
-
isoelectric focusing, pH-range: 3-10
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE