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Information on EC 1.1.3.20 - long-chain-alcohol oxidase
for references in articles please use BRENDA:EC1.1.3.20
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.20 long-chain-alcohol oxidase
IUBMB Comments
Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.1.3.20
- oxidases
- candida
- n-alkanes
- glycolipids
- bombicola
-
dicarboxylic
- cloacae
-
starmerella
- n-hexadecane
-
flavin-containing
-
sophorolipids
-
yarrowia
- lipolytica
- 1-dodecanol
- tropicalis
- alkane
-
obviate
showSynonyms
fatty alcohol oxidase, long chain alcohol oxidase, long-chain fatty alcohol oxidase, long chain fatty alcohol oxidase, fao1p, ljfao1 protein, long-chain fatty acid oxidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alcohol: O2 oxidoreductase
FAO
FAO1
Fao1p
fatty alcohol oxidase
fatty alcohol:oxygen oxidoreductase
-
-
-
-
LCAO
long chain alcohol oxidase
long-chain fatty acid oxidase
-
-
-
-
long-chain fatty alcohol oxidase
oxidase, long-chain fatty alcohol
-
-
-
-
YALI0_B14014g
fatty alcohol oxidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
ping-pong mechanism
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
2 long-chain alcohol + O2 = 2 long-chain aldehyde + 2 H2O2
-
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
alkane oxidation
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SYSTEMATIC NAME
IUBMB Comments
long-chain-alcohol:oxygen oxidoreductase
Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol.
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CAS REGISTRY NUMBER
COMMENTARY
129430-50-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-decanol + O2
decanal + H2O2
Substrates: -
Products: -
Products: -
?
1-docosanol + O2
docosanal + H2O2
-
Substrates: i.e. behenyl alcohol, poor substrate
Products: -
Products: -
?
1-octanol + O2
octanal + H2O2
Substrates: -
Products: -
Products: -
?
12-hydroxydodecanoic acid + O2
?
-
Substrates: poor substrate
Products: -
Products: -
?
2 long-chain alcohol + O2
2 long-chain aldehyde + 2 H2O
-
Substrates: involved in fatty acid metabolism
Products: -
Products: -
?
chrysanthemyl alcohol + O2
chrysanthenmyl aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
cis-11-hexadecenol + O2
cis-11-hexadecenal + H2O2
-
Substrates: -
Products: -
Products: -
?
geraniol + O2
3,7-dimethylocta-trans-2,6-dien-1-al + H2O2
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Substrates: i.e. 3,7-dimethylocta-trans-2,6-dien-1-ol, better substrate than cis-isomer, the 2-ene-group enhances activity
Products: -
Products: -
?
hex-trans-2-ene-1-ol + O2
hex-trans-2-ene-1-al + H2O2
-
Substrates: preferred substrate, the 2-ene-group enhances activity
Products: -
Products: -
?
1,16-hexadecanediol + O2
?
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Substrates: purified active LjFAO1 protein
Products: -
Products: -
?
1-dodecanol + O2
dodecanal + H2O2
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Substrates: purified active LjFAO1 protein
Products: -
Products: -
?
1-dodecanol + O2
dodecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-dodecanol + O2
dodecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-dodecanol + O2
dodecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-dodecanol + O2
dodecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-eicosanol + O2
eicosanal + H2O2
-
Substrates: i.e. arachidyl alcohol, poor substrate
Products: -
Products: -
?
1-hexadecanol + O2
hexadecanal + H2O2
-
Substrates: purified active LjFAO1 protein
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
-
Substrates: 75% the rate of dodecanol oxidation
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
-
Substrates: oxidation at 74% the rate of dodecanol oxidation
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
-
Substrates: i.e. myristyl alcohol, best substrate
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
Substrates: -
Products: -
Products: -
?
1-tetradecanol + O2
tetradecanal + H2O2
Substrates: -
Products: -
Products: -
?
12-bromododecanol + O2
12-bromodecanal + H2O2
-
Substrates: oxidation at 92% the rate of dodecanol oxidation
Products: -
Products: -
?
12-bromododecanol + O2
12-bromodecanal + H2O2
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Substrates: oxidation at the same rate as dodecanol
Products: -
Products: -
?
alpha,omega-alkanediols + O2
?
-
Substrates: from C10 to C16
Products: -
Products: -
?
alpha,omega-alkanediols + O2
?
-
Substrates: from C10 to C16
Products: -
Products: -
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
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Substrates: oxidation at 1.9% the rate of dodecanol oxidation
Products: -
Products: -
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
-
Substrates: higher oxidation rate than saturated analog
Products: -
Products: -
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
-
Substrates: oxidation at 19% the rate of dodecanol oxidation
Products: -
Products: -
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
-
Substrates: -
Products: -
Products: -
?
decanol + O2
decanal + H2O2
-
Substrates: oxidation at 70% the rate of dodecanol oxidation
Products: -
Products: -
?
decanol + O2
decanal + H2O2
-
Substrates: oxidation at 51% the rate of dodecanol oxidation
Products: -
Products: -
?
docosenol + O2
docosenal + H2O2
-
Substrates: oxidation at 13% the rate of dodecanol oxidation
Products: -
Products: -
?
docosenol + O2
docosenal + H2O2
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Substrates: higher oxidation rate than saturated analog
Products: -
Products: -
?
dodecanol + O2
dodecanal + H2O2
-
Substrates: i.e. lauryl alcohol, preferred substrate
Products: -
Products: -
?
dodecanol + O2
dodecanal + H2O2
-
Substrates: i.e. lauryl alcohol, preferred substrate
Products: -
Products: -
?
hexadecanol + O2
hexadecanal + H2O2
-
Substrates: 19% the rate of dodecanol oxidation
Products: -
Products: -
?
hexadecanol + O2
hexadecanal + H2O2
-
Substrates: 68% the rate of dodecanol oxidation
Products: -
Products: -
?
hexadecanol + O2
hexadecanal + H2O2
-
Substrates: i.e. palmityl or cetyl alcohol, oxidation at 26% the rate of dodecanol oxidation
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: reaction in n-alkane catabolism
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: n-alkan-inducible enzyme
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: reaction in wax ester catabolism in the storage wax bodies of jojoba plant during germination
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: monounsaturated long-chain alcohols
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: constitutive enzyme, perhaps two enzymes
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: substrates are primary alcohols with a chain-length of C6-C10
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: n-alkan-inducible enzyme
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
Torulopsis candida
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
Torulopsis candida
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
[Candida] cloacae FERM O-736
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
[Candida] cloacae FERM O-736
-
Substrates: the enzyme oxidizes alcohol substrates with carbon chain length of usually above C6
Products: -
Products: -
?
n-octanol + O2
n-octanal + H2O2
-
Substrates: oxidation at 34% the rate of dodecanol oxidation
Products: -
Products: -
?
octadecanol + O2
octadecanal + H2O2
-
Substrates: oxidation at 12% the rate of dodecanol oxidation
Products: -
Products: -
?
octadecanol + O2
octadecanal + H2O2
-
Substrates: i.e. stearyl alcohol, oxidation at 16% the rate of dodecanol oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: weak activity towards fatty aldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: dodecan-4-ol, dodecan-5-ol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: dodecanal, omega-hydroxydodecanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: geraniol, hexadecan-2-ol, dodecan-5-ol, 2-adamantol, 5-phenylpentan-1-ol, 4-cyclohexylbutan-1-ol, 1-adamantane ethanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: ethanol, palmitic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: ethanol, palmitic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: omega-hydroxy fatty acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: perhaps two long-chain alcohol oxidases in Candida bombicola: the two best substrates are decanol and tetradecanol
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not oxidize 2-alkanols
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not oxidize 2-alkanols
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: 2-dodecanol, 2-tetradecanol, 7-tetradecanol, 2-hexadecanol or secondary alcohols
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not oxidize 2-alkanols
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates are primary alcohols with a chain-length of C6-C10, optimal chain-length: C8-C10
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates for Tanacetum enzyme: secondary, tertiary alcohols and Tris
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme from Tanacetum vulgare oxidizes both the long chains of saturated and unsaturated alcohol substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is active with substrates having a carbon chain length of six and above, showing the highest activity with 1-dodecanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 long-chain alcohol + O2
2 long-chain aldehyde + 2 H2O
-
Substrates: involved in fatty acid metabolism
Products: -
Products: -
?
cis-11-eicosenol + O2
cis-11-eicosenal + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: reaction in n-alkane catabolism
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: n-alkan-inducible enzyme
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: reaction in wax ester catabolism in the storage wax bodies of jojoba plant during germination
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: monounsaturated long-chain alcohols
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: constitutive enzyme, perhaps two enzymes
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: substrates are primary alcohols with a chain-length of C6-C10
Products: -
Products: -
?
long-chain alcohol + O2
?
-
Substrates: n-alkan-inducible enzyme
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
Torulopsis candida
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + O2
long-chain aldehyde + H2O2
[Candida] cloacae FERM O-736
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme from Tanacetum vulgare oxidizes both the long chains of saturated and unsaturated alcohol substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
not FAD, FMN, riboflavin, different absorption and fluorescence emission spectra, flavin is probably covalently bound
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
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
70% loss of activity at 0.1 mM, completely reversible with dithiothreitol
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
-
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
-
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 effects upon addition or deletion of FAD, flavin mononucleotide, NADP+, and NAD+ in the reaction mixture
-
additional information
-
no inhibitors: pyrazole, decanethiol, loss of enzyme activity under anaerobic conditions is reversible by introduction of oxygen
-
additional information
-
no inhibitor: cyanide; no inhibitors: iodoacetate, MnSO4, EDTA, p-hydroxymercuribenzoate, 2,2'-dipyridyl, 1,10-phenanthroline, 8-hydroxyquinoline, fluoride, azide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
0.0277
1-Dodecanol
pH 7.4, 25°C
0.059
1-Dodecanol
-
5 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana
0.049
1-hexadecanol
-
1 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
0.23
substrate 1-dodecanol, pH 7.4, 25°C
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
almost complete loss of activity
6 - 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
higher conversions appear at lower temperatures due to an increased stability of the enzyme
20 - 30
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 45
-
about 60% of maximal activity at 0°C and about 30% of maximal activity at 45°C
45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the oil-contaminated soil sample, collected from an oil field of Assam, enzyme form H3
-
-
brenda
isolated from the oil-contaminated soil sample, collected from an oil field of Assam, enzyme form H3
-
-
brenda
the fungus produces the enzyme during growth on hydrocarbon substrates
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
8-day-old seedlings, RT-PCR, whole plant expression shown, cold stress treatment of
brenda
additional information
additional information
-
the fungus produces the enzyme during growth on hydrocarbon substrates
brenda
additional information
-
evaluation of different carbon sources for growth, overview
brenda
additional information
-
evaluation of different carbon sources for growth, overview
-
brenda
additional information
-
the fungus produces the enzyme during growth on hydrocarbon substrates
brenda
additional information
-
gene FaO1 is expressed in the whole plant, with the highest expression level in the apex
brenda
additional information
-
the fungus produces the enzyme during growth on hydrocarbon substrates
brenda
additional information
-
the fungus produces the enzyme during growth on hydrocarbon substrates
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
sequence contains a predicted membrane binding helix within the substrate binding domain
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
a FAO1 mutant is unable to grow with secondary alcohols, but has very low activity toward secondary alcohols. Alkyl polyglucosides hydroxylated at the omega position in the alkyl chain of the secondary alcohol are observed in the FAO1 mutant. In the double mutant of FAO1 and hydroxy fatty acid glycosyltransferase UGTA1, accumulation of 1,13-tetradecandiol and 2,13-tetradecandiol is observed. Hydroxylation occurs first at the omega and omega-1 positions in the secondary alcohol metabolism of Starmerella bombicola, followed by primary alcohol oxidation
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
metabolism
-
the enzyme is involved in omega-oxidation of long-chain fatty acids
metabolism
-
the enzyme is involved in omega-oxidation of long-chain fatty acids
-
Show AA Sequence and Transmembrane Helices (3043 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
73000
75000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homooctamer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
80
30 min, complete loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
phenylmethylsulfonyl fluoride stabilizes during purification and storage
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen together with light of 450 nm inactivates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, phosphate buffered saline, 25 mM Tris-HCl, pH 7.5, 0.3 M NaCl, 1 mM dithiothreitol, 20% glycerol
-
0C, in the dark stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homogeneity
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme is able to refold and regain its activity upon heating up to 65°C
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moreau, R.A.; Huang, A.H.C.
Enzymes of wax ester catabolism in jojoba
Methods Enzymol.
71
804-813
1981
Simmondsia chinensis
-
brenda
Banthorpe, D.V.; Cardemil, E.; Del Carmen Contraras, M.
Purification and properties of alcohole oxidase from Tanacetum vulgare
Phytochemistry
15
391-394
1976
Tanacetum vulgare
-
brenda
Moreau, R.A.; Huang, A.H.C.
Oxidation of fatty alcohol in the cotyledons of jojoba seedlings
Arch. Biochem. Biophys.
194
422-430
1979
Simmondsia chinensis
brenda
Kemp, G.D.; Dickinson, F.M.; Ratledge, C.
Inducible long chain alcohol oxidase from alkane-grown Candida tropicalis
Appl. Microbiol. Biotechnol.
29
370-374
1988
Candida tropicalis
-
brenda
Hommel, R.; Ratledge, C.
Evidence frr two fatty alcohol oxidases in the biosurfactant-producing yeast Candida (Torulopsis) bombicola
FEMS Microbiol. Lett.
70
183-186
1990
Starmerella bombicola
brenda
Kemp, G.D.; Dickinson, F.M.; Ratledge, C.
Light sensitivity of the n-alkane-induced fatty alcohol oxidase from Candida tropicalis and Yarrowia lipolytica
Appl. Microbiol. Biotechnol.
32
461-464
1990
Candida tropicalis, Yarrowia lipolytica
-
brenda
Kemp, G.D.; Dickinson, F.M.; Ratledge, C.
Activity and substrate specificity of the fatty alcohol oxidase of Candida tropicalis in organic solvents
Appl. Microbiol. Biotechnol.
34
441-445
1991
Candida tropicalis
-
brenda
Dickinson, F.M.; Wadforth, C.
Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis
Biochem. J.
282
325-331
1992
Candida tropicalis
brenda
Vanhanen, S.; West, M.; Kroon, J.T.M.; Lindner, N.; Casey, J.; Cheng, Q.; Elborough, K.M.; Slabas, A.R.
A consensus sequence for long-chain fatty-acid alcohol oxidases from Candida identifies a family of genes involved in lipid.omega-oxidation in yeast with homologues in plants and bacteria
J. Biol. Chem.
275
4445-4452
2000
[Candida] cloacae, [Candida] cloacae 3152
brenda
Il'chenko, A.P.; Morgunov, I.G.; Honeck, H.; Mauersberger, S.; Vasilkova, N.N.; Muller, H.G.
Purification and some properties of alcohol oxidase from the yeast Yarrowia lipolytica H-222
Biokhimiya
59
1312-1319
1994
Yarrowia lipolytica, Yarrowia lipolytica H-222
-
brenda
Cheng, Q.; Liu, H.T.; Bombelli, P.; Smith, A.; Slabas, A.R.
Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana
FEBS Lett.
574
62-68
2004
Arabidopsis thaliana
brenda
Kumar, A.K.; Goswami, P.
Functional characterization of alcohol oxidases from Aspergillus terreus MTCC 6324
Appl. Microbiol. Biotechnol.
72
906-911
2006
Aspergillus terreus, Aspergillus terreus MTCC 6324
brenda
Cheng, Q.; Sanglard, D.; Vanhanen, S.; Liu, H.T.; Bombelli, P.; Smith, A.; Slabas, A.R.
Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism
Biochim. Biophys. Acta
1735
192-203
2005
Candida tropicalis, [Candida] cloacae
brenda
Zhao, S.; Lin, Z.; Ma, W.; Luo, D.; Cheng, Q.
Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in lotus japonicus
Biotechnol. Prog.
24
773-779
2008
Lotus japonicus
brenda
Silva-Jimenez, H.; Zazueta-Novoa, V.; Duron-Castellanos, A.; Rodriguez-Robelo, C.; Leal-Morales, C.A.; Zazueta-Sandoval, R.
Intracellular distribution of fatty alcohol oxidase activity in Mucor circinelloides YR-1 isolated from petroleum contaminated soils
Antonie van Leeuwenhoek
96
527-535
2009
Mucor circinelloides, Mucor circinelloides YR-1
brenda
Goswami, P.; Chinnadayyala, S.S.; Chakraborty, M.; Kumar, A.K.; Kakoti, A.
An overview on alcohol oxidases and their potential applications
Appl. Microbiol. Biotechnol.
97
4259-4275
2013
Arabidopsis thaliana, Aspergillus sp., Aspergillus terreus, Candida tropicalis, Candida tropicalis NCYC 470, Cladosporium sp., Lotus japonicus, Meyerozyma guilliermondii, Mucor circinelloides, Mucor circinelloides YR-1, Simmondsia chinensis, Starmerella apicola, Starmerella bombicola, Tanacetum vulgare, Torulopsis candida, Yarrowia lipolytica, [Candida] cloacae, [Candida] cloacae FERM O-736
brenda
Takahashi, F.; Igarashi, K.; Hagihara, H.
Identification of the fatty alcohol oxidase FAO1 from Starmerella bombicola and improved novel glycolipids production in an FAO1 knockout mutant
Appl. Microbiol. Biotechnol.
100
9519-9528
2016
Starmerella bombicola (A0A024FB95), Starmerella bombicola, Starmerella bombicola KSM36 (A0A024FB95)
brenda
Gatter, M.; Foerster, A.; Baer, K.; Winter, M.; Otto, C.; Petzsch, P.; Jezkova, M.; Bahr, K.; Pfeiffer, M.; Matthaeus, F.; Barth, G.
A newly identified fatty alcohol oxidase gene is mainly responsible for the oxidation of long-chain omega-hydroxy fatty acids in Yarrowia lipolytica
FEMS Yeast Res.
14
858-872
2014
Yarrowia lipolytica, Yarrowia lipolytica H222
brenda
Iwama, R.; Kobayashi, S.; Ohta, A.; Horiuchi, H.; Fukuda, R.
Alcohol dehydrogenases and an alcohol oxidase involved in the assimilation of exogenous fatty alcohols in Yarrowia lipolytica
FEMS Yeast Res.
15
fov014
2015
Yarrowia lipolytica (Q6CEP8), Yarrowia lipolytica, Yarrowia lipolytica CXAU/A1 (Q6CEP8)
brenda
Rembeza, E.; Boverio, A.; Fraaije, M.W.; Engqvist, M.K.M.
Discovery of two novel oxidases using a high-throughput activity screen
Chembiochem
23
e202100510
2022
uncultured marine group II/III euryarchaeote KM3_72_H01 (A0A075HNX4)
brenda
Takahashi, F.; Igarashi, K.; Takimura, Y.; Yamamoto, T.
Elucidation of secondary alcohol metabolism in Starmerella bombicola and contribution of primary alcohol oxidase FAO1
FEMS Yeast Res.
19
foz012
2019
Starmerella bombicola (A0A024FB95)
brenda
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