Information on EC 1.1.3.20 - long-chain-alcohol oxidase

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:
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
1.1.3.20
-
RECOMMENDED NAME
GeneOntology No.
long-chain-alcohol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2; ping-pong mechanism
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
long-chain-alcohol:oxygen oxidoreductase
Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alcohol: O2 oxidoreductase
Candida cloacae FERM O-736
-
-
-
alcohol: O2 oxidoreductase
-
-
alcohol: O2 oxidoreductase
Candida tropicalis NCYC 470
-
-
-
alcohol: O2 oxidoreductase
-
-
alcohol: O2 oxidoreductase
Mucor circinelloides YR-1
-
-
-
alcohol: O2 oxidoreductase
-
-
FAO
Candida cloacae FERM O-736
-
-
-
FAO
Candida tropicalis NCYC 470
-
-
-
FAO
Mucor circinelloides YR-1
-
;
-
fatty alcohol oxidase
-
-
-
-
fatty alcohol oxidase
-
-
fatty alcohol oxidase
-
-
fatty alcohol oxidase
Aspergillus terreus MTCC 6324
-
-
-
fatty alcohol oxidase
-
-
fatty alcohol oxidase
Candida cloacae FERM O-736
-
-
-
fatty alcohol oxidase
-
-
fatty alcohol oxidase
Candida tropicalis NCYC 470
-
-
-
fatty alcohol oxidase
-
-
fatty alcohol oxidase
-
-
fatty alcohol oxidase
Mucor circinelloides YR-1
-
;
-
fatty alcohol:oxygen oxidoreductase
-
-
-
-
LCAO
Aspergillus terreus MTCC 6324
-
-
-
LCAO
Candida cloacae FERM O-736
-
-
-
LCAO
Candida tropicalis NCYC 470
-
-
-
LCAO
Mucor circinelloides YR-1
-
-
-
LjFAO1 protein
-
-
long chain alcohol oxidase
-
-
long chain alcohol oxidase
-
-
long chain alcohol oxidase
Aspergillus terreus MTCC 6324
-
-
-
long chain alcohol oxidase
-
-
long chain alcohol oxidase
Candida cloacae FERM O-736
-
-
-
long chain alcohol oxidase
-
-
long chain alcohol oxidase
Candida tropicalis NCYC 470
-
-
-
long chain alcohol oxidase
-
-
long chain alcohol oxidase
Mucor circinelloides YR-1
-
-
-
long chain alcohol oxidase
-
-
long chain fatty acid oxidase
-
-
long chain fatty acid oxidase
Aspergillus terreus MTCC 6324
-
-
-
long chain fatty alcohol oxidase
-
-
long chain fatty alcohol oxidase
Aspergillus terreus MTCC 6324
-
-
-
long-chain fatty acid oxidase
-
-
-
-
long-chain fatty alcohol oxidase
-
-
oxidase, long-chain fatty alcohol
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
129430-50-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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
the fungus produces the enzyme during growth on hydrocarbon substrates
-
-
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324
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
multiple isoforms
-
-
Manually annotated by BRENDA team
strain 3152
-
-
Manually annotated by BRENDA team
two genes FAO1 and FAO2
-
-
Manually annotated by BRENDA team
Candida cloacae 3152
strain 3152
-
-
Manually annotated by BRENDA team
Candida cloacae FERM O-736
two genes FAO1 and FAO2
-
-
Manually annotated by BRENDA team
multiple isoforms
-
-
Manually annotated by BRENDA team
singe gene FAO
-
-
Manually annotated by BRENDA team
Candida tropicalis NCYC 470
singe gene FAO
-
-
Manually annotated by BRENDA team
Cladosporium sp.
-
-
-
Manually annotated by BRENDA team
ecotype Gifu B-129
-
-
Manually annotated by BRENDA team
gene LjFAO1
-
-
Manually annotated by BRENDA team
Mucor circinelloides YR-1
-
-
-
Manually annotated by BRENDA team
syn. Torulopsis bombicola
-
-
Manually annotated by BRENDA team
Torulopsis candida
-
-
-
Manually annotated by BRENDA team
strain H-222
-
-
Manually annotated by BRENDA team
Yarrowia lipolytica H-222
strain H-222
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
1,16-hexadecanediol + O2
?
show the reaction diagram
-
purified active LjFAO1 protein
-
-
?
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-dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
-
-
-
?
1-dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
purified active LjFAO1 protein
-
-
?
1-eicosanol + O2
eicosanal + H2O2
show the reaction diagram
-
-
-
-
?
1-eicosanol + O2
eicosanal + H2O2
show the reaction diagram
-
i.e. arachidyl alcohol, poor substrate
-
-
?
1-hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
-
-
-
?
1-hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
-
-
-
?
1-hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
purified active LjFAO1 protein
-
-
?
1-tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
-
-
-
?
1-tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
-
-
-
?
1-tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
-
oxidation at 74% the rate of dodecanol oxidation
-
-
?
1-tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
-
75% the rate of dodecanol oxidation
-
-
?
1-tetradecanol + O2
tetradecanal + H2O2
show the reaction diagram
-
i.e. myristyl alcohol, best substrate
-
-
?
12-bromododecanol + O2
12-bromodecanal + H2O2
show the reaction diagram
-
oxidation at 92% the rate of dodecanol oxidation
-
-
?
12-bromododecanol + O2
12-bromodecanal + H2O2
show the reaction diagram
-
oxidation at the same rate as dodecanol
-
-
?
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
-
from C10 to C16
-
-
?
alpha,omega-alkanediols + O2
?
show the reaction diagram
-
from C10 to C16
-
-
?
chrysanthemyl alcohol + O2
chrysanthenmyl aldehyde + H2O2
show the reaction diagram
-
-
-
-
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
show the reaction diagram
-
-
-
-
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
show the reaction diagram
-
higher oxidation rate than saturated analog
-
-
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
show the reaction diagram
-
oxidation at 19% the rate of dodecanol oxidation
-
-
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
show the reaction diagram
-
oxidation at 1.9% the rate of dodecanol oxidation
-
-
?
cis-11-hexadecenol + O2
cis-11-hexadecenal + H2O2
show the reaction diagram
-
-
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
-
-
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
-
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
-
best substrate
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
-
oxidation at 70% the rate of dodecanol oxidation
-
-
?
decanol + O2
decanal + H2O2
show the reaction diagram
-
oxidation at 51% the rate of dodecanol oxidation
-
-
?
diol + O2
?
show the reaction diagram
-
poor substrates
-
-
?
diol + O2
?
show the reaction diagram
-
e.g. hexadecan-1,16-diol has an oxidation rate at 31% the rate of dodecanol oxidation
-
-
?
docosenol + O2
docosenal + H2O2
show the reaction diagram
-
-, oxidation at 13% the rate of dodecanol oxidation
-
-
?
docosenol + O2
docosenal + H2O2
show the reaction diagram
-
higher oxidation rate than saturated analog
-
-
?
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
-
-
-
?
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
i.e. lauryl alcohol, preferred substrate
-
?
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
i.e. lauryl alcohol, preferred substrate
-
-
?
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
i.e. lauryl alcohol, preferred substrate
-
-
?
dodecanol + O2
dodecanal + H2O2
show the reaction diagram
-
i.e. lauryl alcohol, preferred substrate
-
?
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
-
-
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
-
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
-
-
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
19% the rate of dodecanol oxidation
-
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
68% the rate of dodecanol oxidation
-
-
?
hexadecanol + O2
hexadecanal + H2O2
show the reaction diagram
-
i.e. palmityl or cetyl alcohol, oxidation at 26% the rate of dodecanol oxidation
-
-
?
hexanol + O2
hexanal + H2O2
show the reaction diagram
-
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
-
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
-
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
reaction in wax ester catabolism in the storage wax bodies of jojoba plant during germination
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
substrates are primary alcohols with a chain-length of C6-C10
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
reaction in n-alkane catabolism
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
n-alkan-inducible enzyme
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
n-alkan-inducible enzyme
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
monounsaturated long-chain alcohols
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
constitutive enzyme, perhaps two enzymes
-
-
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
-
the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
-
-
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
Mucor circinelloides YR-1
-
-, the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
-
-
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
Candida cloacae FERM O-736
-
-, the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
-
-
?
n-octanol + O2
n-octanal + H2O2
show the reaction diagram
-
-
-
?
n-octanol + O2
n-octanal + H2O2
show the reaction diagram
-
-
-
?
n-octanol + O2
n-octanal + H2O2
show the reaction diagram
-
-
-
-
?
n-octanol + O2
n-octanal + H2O2
show the reaction diagram
-
oxidation at 34% the rate of dodecanol oxidation
-
-
?
octadecanol + O2
octadecanal + H2O2
show the reaction diagram
-
-
-
?
octadecanol + O2
octadecanal + H2O2
show the reaction diagram
-
-
-
?
octadecanol + O2
octadecanal + H2O2
show the reaction diagram
-
oxidation at 12% the rate of dodecanol oxidation
-
-
?
octadecanol + O2
octadecanal + H2O2
show the reaction diagram
-
i.e. stearyl alcohol, oxidation at 16% the rate of dodecanol oxidation
-
-
?
terpenol + O2
?
show the reaction diagram
-
poor substrate
-
-
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
Candida tropicalis NCYC 470
-
-, the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
-
-
?
additional information
?
-
-
weak activity towards fatty aldehydes
-
-
-
additional information
?
-
-
no substrate: omega-hydroxy fatty acids
-
-
-
additional information
?
-
-
no substrate: dodecan-4-ol, dodecan-5-ol
-
-
-
additional information
?
-
-
substrates are primary alcohols with a chain-length of C6-C10, optimal chain-length: C8-C10
-
-
-
additional information
?
-
-
no substrates: dodecanal, omega-hydroxydodecanoate
-
-
-
additional information
?
-
-
perhaps two long-chain alcohol oxidases in Candida bombicola: the two best substrates are decanol and tetradecanol
-
-
-
additional information
?
-
-
no substrates for Tanacetum enzyme: secondary, tertiary alcohols and Tris
-
-
-
additional information
?
-
-
no substrates: ethanol, palmitic acid
-
-
-
additional information
?
-
-
no substrate: geraniol, hexadecan-2-ol, dodecan-5-ol, 2-adamantol, 5-phenylpentan-1-ol, 4-cyclohexylbutan-1-ol, 1-adamantane ethanol
-
-
-
additional information
?
-
-
the enzyme is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism
-
-
-
additional information
?
-
-
the enzyme is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism, different pathways of octadecane, hexadecane, oleic acid and palmitic acid utilization exist in the organism, overview
-
-
-
additional information
?
-
-
the fungal enzyme forms H1, H2, H3, and H4 have similar biochemical properties, but show different substrate specificities from short chain alcohol oxidase for H1, aryl alcohol oxidase for H4, and secondary alcohol oxidase for H2, H3 is a long chain alcohol oxidase, overview
-
-
-
additional information
?
-
-
the enzyme from Tanacetum vulgare oxidizes both the long chains of saturated and unsaturated alcohol substrates
-
-
-
additional information
?
-
Aspergillus terreus MTCC 6324
-
the fungal enzyme forms H1, H2, H3, and H4 have similar biochemical properties, but show different substrate specificities from short chain alcohol oxidase for H1, aryl alcohol oxidase for H4, and secondary alcohol oxidase for H2, H3 is a long chain alcohol oxidase, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
?
show the reaction diagram
-
-
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
reaction in wax ester catabolism in the storage wax bodies of jojoba plant during germination
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
substrates are primary alcohols with a chain-length of C6-C10
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
reaction in n-alkane catabolism
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
n-alkan-inducible enzyme
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
n-alkan-inducible enzyme
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
monounsaturated long-chain alcohols
-
-
?
long-chain alcohol + O2
?
show the reaction diagram
-
constitutive enzyme, perhaps two enzymes
-
-
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism
-
-
-
additional information
?
-
-
the enzyme is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism, different pathways of octadecane, hexadecane, oleic acid and palmitic acid utilization exist in the organism, overview
-
-
-
additional information
?
-
-
the enzyme from Tanacetum vulgare oxidizes both the long chains of saturated and unsaturated alcohol substrates
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
flavin
-
not FAD, FMN, riboflavin, different absorption and fluorescence emission spectra, flavin is probably covalently bound
flavin
-
enzyme-bound, dependent on
additional information
-
FAD, FMN; NAD(P)+
-
additional information
-
no cofactor: riboflavin, 2,6-dichlorophenolindophenol/phenazine methosulfate, potassium ferricyanide, cytochrome c, nitro blue tetrazolium, tetramethyl-p-phenylenediamine
-
additional information
-
no effects upon addition or deletion of FAD, flavin mononucleotide, NADP+, and NAD+ in the reaction mixture
-
additional information
-
NAD(P)+
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
-
-
light
-
enzyme from Yarrowia more sensitive to light than Candida tropicalis, inactivation diminished under anaerobic conditions, light of wavelength longer than 480 nm and shorter than 430 nm does not inactivate; photochemical inactivation at wavelength of 450 nm, i.e. blue-light region of the spectrum of visible light
-
light
-
complete inactivation, t1/2: 7 min; photochemical inactivation at wavelength of 450 nm, i.e. blue-light region of the spectrum of visible light
-
light
-
LCAO activity from n-alkane-grown Candida tropicalis rapidly decreases on exposure to light. The rate of inactivation of the enzyme depends upon the intensity and wavelength of the incident light, but is diminished under anaerobic conditions
-
O2
-
together with light of 405 nm photochemical inactivation
p-chloromercuribenzoate
-
70% loss of activity at 0.1 mM, completely reversible with dithiothreitol
light
-
LCAO activity from n-alkane-grown Yarrowia lipolytica rapidly decreases on exposure to light. The rate of inactivation of the enzyme depends upon the intensity and wavelength of the incident light, but is diminished under anaerobic conditions
-
additional information
-
no inhibitor: cyanide; no inhibitors: iodoacetate, MnSO4, EDTA, p-hydroxymercuribenzoate, 2,2'-dipyridyl, 1,10-phenanthroline, 8-hydroxyquinoline, fluoride, azide
-
additional information
-
no inhibitors: pyrazole, decanethiol, loss of enzyme activity under anaerobic conditions is reversible by introduction of oxygen
-
additional information
-
no effects upon addition or deletion of FAD, flavin mononucleotide, NADP+, and NAD+ in the reaction mixture
-
additional information
-
no inhibitor: cyanide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
1-Dodecanol
-
5 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana
0.0596
-
1-Dodecanol
-
pH and temperature not specified in the publication
0.0409
-
1-hexadecanol
-
pH and temperature not specified in the publication
0.049
-
1-hexadecanol
-
1 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana
0.042
-
Decanol
-
-
0.004
-
Dodecanol
-
-
0.0061
-
Dodecanol
-
-
0.008
-
Dodecanol
-
aqueous phase
4
-
Dodecanol
-
-
40
-
Dodecanol
-
octane/aqueous phase 99/1
1.56
-
geraniol
-
-
0.19
-
Hex-trans-2-ene-1-ol
-
-
0.005
-
hexadecanol
-
-
0.49
-
n-Octanol
-
value above
0.0015
-
Tetradecanol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9
-
plateau
7.6
8.8
-
decanol
8.1
8.3
-
tetradecanol
9
-
-
1-dodecanol
9
-
-
60% activity at pH 7.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
10
-
about half-maximal activity at pH 4.8 and 10.0
6.6
9.3
-
about half-maximal activity at pH 6.6 and 9.3
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
higher conversions appear at lower temperatures due to an increased stability of the enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.5
-
high activity
6
-
-
the enzyme has two isoelectric point components: 6.0 and 6.3, isoelectric focusing
6.3
-
-
the enzyme has two isoelectric point components: 6.0 and 6.3, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Mucor circinelloides YR-1
-
-
-
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324
-
-
-
Manually annotated by BRENDA team
-
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
-
evaluation of different carbon sources for growth, overview
Manually annotated by BRENDA team
additional information
Aspergillus sp., Cladosporium sp.
-
the fungus produces the enzyme during growth on hydrocarbon substrates
Manually annotated by BRENDA team
additional information
-
gene FaO1 is expressed in the whole plant, with the highest expression level in the apex
Manually annotated by BRENDA team
additional information
-
the fungus produces the enzyme during growth on hydrocarbon substrates
Manually annotated by BRENDA team
additional information
Aspergillus terreus MTCC 6324
-
evaluation of different carbon sources for growth, overview
-
Manually annotated by BRENDA team
additional information
Mucor circinelloides YR-1
-
the fungus produces the enzyme during growth on hydrocarbon substrates
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Candida cloacae FERM O-736, Candida tropicalis NCYC 470, Mucor circinelloides YR-1
-
-
-
Manually annotated by BRENDA team
-
located on the inner face of the membrane
Manually annotated by BRENDA team
Tanacetum vulgare, Torulopsis candida
-
-
Manually annotated by BRENDA team
Candida cloacae FERM O-736, Candida tropicalis NCYC 470
-
-
-
Manually annotated by BRENDA team
Mucor circinelloides YR-1
-
; located on the inner face of the membrane
-
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324, Candida cloacae 3152, Candida cloacae FERM O-736, Candida tropicalis NCYC 470, Mucor circinelloides YR-1
-
-
-
-
Manually annotated by BRENDA team
Candida cloacae FERM O-736, Candida tropicalis NCYC 470, Mucor circinelloides YR-1
-
-
-
Manually annotated by BRENDA team
Mucor circinelloides YR-1
-
;
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
73000
-
-
SDS-PAGE
73000
-
-
recombinant protein, SDS-PAGE
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 ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
1 * 94000 + 1 * 75000, SDS-PAGE
dimer
-
2 * 70000, SDS-PAGE
heterodimer
Candida cloacae FERM O-736, Candida tropicalis NCYC 470
-
-
-
homooctamer
-
8 * 46000, SDS-PAGE
homooctamer
Mucor circinelloides YR-1
-
8 * 46000, SDS-PAGE
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
inactivation after 3 min
7
-
-
and below unstable
9
-
-
at least 15 min stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
at least 15 min stable
25
-
-
inactivation overnight
30
-
-
rapid loss of activity
30
-
-
unstable above
37
-
-
inactivation after 1 min
100
-
-
boiling for 30 min inactivates the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
stable to
octane
-
enzyme stable in 99% octane/1% H2O
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxygen together with light of 450 nm inactivates
-
389736
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
0C, in the dark stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein using His-tag
-
homogeneity
-
full length version of LjFAO1 protein, gel purification
-
homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed as a His-tagged protein in Escherichia coli
-
two genes FAO1 and FAO2, DNA and amino acid sequence determination and analysis, sequence comparison
-
single gene FAO, DNA and amino acid sequence determination and analysis, sequence comparison
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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