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
methanol oxidation to formaldehyde IV
-
-
methane metabolism
-
-
Methane metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
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
Pichia putida
-
3% activity compared to methanol
-
-
?
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
-
-
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 - 20.2
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
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 OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7
-
ethanol oxidation
5.5 - 8.5
-
-
6 - 10
broad optimum
6.3 - 9
-
-
6.5
-
assay at
7.4
-
assay at
7.5 - 9.5
-
-
8.5 - 9
Pichia putida
-
-
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
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
SOURCE
the enzyme is localized in the hyphal periplasmic space and wall and on extracellular tripartite membranes and slime, while there is no labeling of hyphal peroxisomes. AOX is associated with membranous or slime structures secreted by hyphae in wood fiber lumina and within the secondary cell walls of degraded wood fibers
Manually annotated by BRENDA team
additional information