Information on EC 1.1.3.20 - long-chain-alcohol oxidase

New: Word Map on EC 1.1.3.20
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
1.1.3.20
-
RECOMMENDED NAME
GeneOntology No.
long-chain-alcohol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alkane oxidation
-
-
SYSTEMATIC NAME
IUBMB Comments
long-chain-alcohol:oxygen oxidoreductase
Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
CAS REGISTRY NUMBER
COMMENTARY hide
129430-50-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain MTCC 6324, isolated from the oil-contaminated soil sample, collected from an oil field of Assam, enzyme form H3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 3152
-
-
Manually annotated by BRENDA team
Candida cloacae FERM O-736
two genes FAO1 and FAO2
-
-
Manually annotated by BRENDA team
singe gene FAO
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Torulopsis candida
-
-
-
Manually annotated by BRENDA team
strain H-222
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the cotyledons of Simmondsia chinensis containing FAO and fatty alcohol dehydrogenase also oxidize fatty alcohols formed from the hydrolysis of stored wax esters during germination
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,10-decanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,14-tetradecanediol + O2
?
show the reaction diagram
-
-
-
-
?
1,16-hexadecandiol + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
1,16-hexadecanediol + O2
?
show the reaction diagram
1-docosanol + O2
docosanal + H2O2
show the reaction diagram
-
i.e. behenyl alcohol, poor substrate
-
-
?
1-dodecanol + O2
dodecanal + H2O2
show the reaction diagram
1-eicosanol + O2
eicosanal + H2O2
show the reaction diagram
1-hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
1-tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
12-bromododecanol + O2
12-bromodecanal + H2O2
show the reaction diagram
12-hydroxydodecanoic acid + O2
?
show the reaction diagram
-
poor substrate
-
-
?
16-hydroxyhexadecanoic acid + O2
?
show the reaction diagram
-
-
-
-
?
2 long-chain alcohol + O2
2 long-chain aldehyde + 2 H2O
show the reaction diagram
-
involved in fatty acid metabolism
-
-
?
2-dodecanol + O2
?
show the reaction diagram
-
-
-
-
?
alpha,omega-alkanediols + O2
?
show the reaction diagram
chrysanthemyl alcohol + O2
chrysanthenmyl aldehyde + H2O2
show the reaction diagram
-
-
-
-
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
show the reaction diagram
cis-11-hexadecenol + O2
cis-11-hexadecenal + H2O2
show the reaction diagram
-
-
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
diol + O2
?
show the reaction diagram
docosenol + O2
docosenal + H2O2
show the reaction diagram
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
farnesol + O2
farnesal + H2O2
show the reaction diagram
-
-
-
-
?
geraniol + O2
3,7-dimethylocta-trans-2,6-dien-1-al + H2O2
show the reaction diagram
-
i.e. 3,7-dimethylocta-trans-2,6-dien-1-ol, better substrate than cis-isomer, the 2-ene-group enhances activity
-
-
?
hex-trans-2-ene-1-ol + O2
hex-trans-2-ene-1-al + H2O2
show the reaction diagram
-
preferred substrate, the 2-ene-group enhances activity
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
hexanol + O2
hexanal + H2O2
show the reaction diagram
-
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
n-octanol + O2
n-octanal + H2O2
show the reaction diagram
octadecanol + O2
octadecanal + H2O2
show the reaction diagram
terpenol + O2
?
show the reaction diagram
-
poor substrate
-
-
?
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
1,16-hexadecandiol + O2
? + H2O2
show the reaction diagram
-
-
-
-
?
1-dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
-
-
-
?
1-hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
-
-
-
?
2 long-chain alcohol + O2
2 long-chain aldehyde + 2 H2O
show the reaction diagram
-
involved in fatty acid metabolism
-
-
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
show the reaction diagram
-
-
-
-
?
docosenol + O2
docosenal + H2O2
show the reaction diagram
-
-
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
70% loss of activity at 0.1 mM, completely reversible with dithiothreitol
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Detergents
-
e.g. cholate, activation, purified preparations do not need detergents for activation
additional information
-
no effects upon addition or deletion of FAD, flavin mononucleotide, NADP+, and NAD+ in the reaction mixture
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0194
1,16-hexadecandiol
-
pH and temperature not specified in the publication
0.019
1,16-hexadecanediol
-
1 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana
0.059 - 0.0596
1-Dodecanol
0.0409 - 0.049
1-hexadecanol
0.042
Decanol
-
-
0.004 - 40
Dodecanol
1.56
geraniol
-
-
0.19
Hex-trans-2-ene-1-ol
-
-
0.005
hexadecanol
-
-
0.49
n-Octanol
-
value above
0.061
O2
-
-
1
Octanol
-
-
0.0015
Tetradecanol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.034
-
hexadecanol
0.035
-
16-hydroxy-hexadecanoate
0.042
-
glucose grown, tetradecanol
0.08
-
dodecanol
0.144
-
n-hexane grown, tetradecanol
0.192
-
cis-11-hexadecanol
0.218
-
dodecanol
0.22
-
decanol, in aqueous phase
additional information
-
LjFAO1 gene identified, genomic structure and mRNA expression, cold stress profiling of LjFAO1 transcripts, overexpression of full-lenght and C-truncated cDNAs, full-length version but not C-truncated part of overexpressed LjFAO1-gene shows long-chain fatty alcohol oxidase activity, substrate specificites of purified protein shown
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
plateau
7.6 - 8.8
-
decanol
8.1 - 8.3
-
tetradecanol
8.5 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 10
-
about half-maximal activity at pH 4.8 and 10.0
6 - 9.5
6.6 - 9.3
-
about half-maximal activity at pH 6.6 and 9.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
20
-
higher conversions appear at lower temperatures due to an increased stability of the enzyme
20 - 30
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 45
-
about 60% of maximal activity at 0C and about 30% of maximal activity at 45C
18 - 35
-
about 60% of maximal activity at 18C and 35C, decanol
20 - 38
-
about half-maximal activity at 20C and 38C, tetradecanol
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
the enzyme has two isoelectric point components: 6.0 and 6.3, isoelectric focusing
6 - 9.5
-
high activity
6.3
-
the enzyme has two isoelectric point components: 6.0 and 6.3, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
8-day-old seedlings, RT-PCR, whole plant expression shown, cold stress treatment of
Manually annotated by BRENDA team
-
lowest mRNA expression in
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77300
-
calculated from amino acid sequence
145000
-
gel filtration
180000
-
gel filtration
272000
-
isozymes H2, H3, and H4, native PAGE
350000
-
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
homooctamer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
inactivation after 3 min
389738
7
-
and below unstable
389738
9
-
at least 15 min stable
389738
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
inactivation after 1 min
100
-
boiling for 30 min inactivates the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CHAPS, 0.5%, stabilizes during solubilization
-
cholate, 1%, solubilizes and stabilizes
-
lyophilization, membrane preparation stable to
-
phenylmethylsulfonyl fluoride stabilizes during purification and storage
-
prolonged dialysis against EDTA, stable to
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
-
stable to
octane
-
enzyme stable in 99% octane/1% H2O
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen together with light of 450 nm inactivates
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, phosphate buffered saline, 25 mM Tris-HCl, pH 7.5, 0.3 M NaCl, 1 mM dithiothreitol, 20% glycerol
-
0C, in the dark stable
0C, in the dark stable for at least 10 h
-
freezing overnight leads to 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
full length version of LjFAO1 protein, gel purification
-
homogeneity
partial
recombinant protein using His-tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged protein in Escherichia coli
-
full length cDNA and C-terminal deleted protein overexpressed in Escherichia coli BL21(DE3), pET-28a and pGEM-T easy plasmids
-
gene LjFAO1, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
single gene FAO, DNA and amino acid sequence determination and analysis, sequence comparison
-
two genes FAO1 and FAO2, DNA and amino acid sequence determination and analysis, sequence comparison
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of a faot double knockout mutant, which shows no enzyme activity and is unable to grow on octadecane, but grows on oleic acid and hexadecane, overview
Show AA Sequence (299 entries)
Please use the Sequence Search for a certain query.