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Information on EC 1.14.14.B9 - fatty acid omega2/3-hydroxyase
for references in articles please use BRENDA:EC1.14.14.B9
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.B9 fatty acid omega2/3-hydroxyase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
CYP4F11, CYP4F12, CYP4F40, CYP4F8, CYP4Z1, cytochrome P450 4F11, cytochrome P450 4F40, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP4F11
CYP4F12
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,10Z,13Z,16Z)-19,20-epoxydocosa-4,7,10,13,16-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,10Z,16Z,19Z)-13,14-epoxydocosa-4,7,10,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,13Z,16Z,19Z)-10,11-epoxydocosa-4,7,13,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,10Z,13Z,16Z)-19,20-epoxydocosa-4,7,10,13,16-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(1)
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,10Z,13Z,16Z)-19,20-epoxydocosa-4,7,10,13,16-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
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(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,10Z,16Z,19Z)-13,14-epoxydocosa-4,7,10,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(2)
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,10Z,16Z,19Z)-13,14-epoxydocosa-4,7,10,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
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(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,13Z,16Z,19Z)-10,11-epoxydocosa-4,7,13,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
(3)
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2 = (4Z,7Z,13Z,16Z,19Z)-10,11-epoxydocosa-4,7,13,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
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SYSTEMATIC NAME
IUBMB Comments
fatty acid,[NADPH-hemoprotein reductase]:oxygen oxidoreductase omega2/3-hydroxylating
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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
(4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate + [reduced NADPH-hemoprotein reductase] + O2
(4Z,7Z,10Z,13Z,16Z)-20-hydroxydocosa-4,7,10,13,16-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: main product, plus minor amounts of 21-hydroxy-4,7,10,13,16-(Z)-docosapentaenoic acid, no significant formation of dihydroxycompounds
Products: main product, plus minor amounts of 21-hydroxy-4,7,10,13,16-(Z)-docosapentaenoic acid, no significant formation of dihydroxycompounds
?
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2
(4Z,7Z,10Z,13Z,16Z)-19,20-epoxydocosa-4,7,10,13,16-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosahexaenoic acid, 13,14-epoxydocosahexaenoic acid, and 10,11-epoxydocosahexaenoic acid, no significant formation of 21-hydroxy- or 22-hydroxydocosahexaenoic acid. Reaction is catalyzed by both isoforms CYP4F8 and CYP4F12
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosahexaenoic acid, 13,14-epoxydocosahexaenoic acid, and 10,11-epoxydocosahexaenoic acid, no significant formation of 21-hydroxy- or 22-hydroxydocosahexaenoic acid. Reaction is catalyzed by both isoforms CYP4F8 and CYP4F12
?
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2
(4Z,7Z,10Z,16Z,19Z)-13,14-epoxydocosa-4,7,10,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosahexaenoic acid, 13,14-epoxydocosahexaenoic acid, and 10,11-epoxydocosahexaenoic acid, no significant formation of 21-hydroxy- or 22-hydroxydocosahexaenoic acid. Reaction is catalyzed by both isoforms CYP4F8 and CYP4F12
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosahexaenoic acid, 13,14-epoxydocosahexaenoic acid, and 10,11-epoxydocosahexaenoic acid, no significant formation of 21-hydroxy- or 22-hydroxydocosahexaenoic acid. Reaction is catalyzed by both isoforms CYP4F8 and CYP4F12
?
(4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate + [reduced NADPH-hemoprotein reductase] + O2
(4Z,7Z,13Z,16Z,19Z)-10,11-epoxydocosa-4,7,13,16,19-pentaenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosahexaenoic acid, 13,14-epoxydocosahexaenoic acid, and 10,11-epoxydocosahexaenoic acid, no significant formation of 21-hydroxy- or 22-hydroxydocosahexaenoic acid. Reaction is catalyzed by both isoforms CYP4F8 and CYP4F12
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosahexaenoic acid, 13,14-epoxydocosahexaenoic acid, and 10,11-epoxydocosahexaenoic acid, no significant formation of 21-hydroxy- or 22-hydroxydocosahexaenoic acid. Reaction is catalyzed by both isoforms CYP4F8 and CYP4F12
?
(7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoate + [reduced NADPH-hemoprotein reductase] + O2
(7Z,10Z,13Z,16Z)-19,20-epoxydocosa-7,10,13,16-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: formation of 19,20-epoxydocosatetraenoic acid, 16,17-epoxydocosatetraenoic acid, 13,14-epoxydocosatetraenoic acid, and 10,11-epoxydocosatetraenoic acid, no formation of 21-hydroxy- or 22-hydroxydocosapentaenoic acid
Products: formation of 19,20-epoxydocosatetraenoic acid, 16,17-epoxydocosatetraenoic acid, 13,14-epoxydocosatetraenoic acid, and 10,11-epoxydocosatetraenoic acid, no formation of 21-hydroxy- or 22-hydroxydocosapentaenoic acid
?
(7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoate + [reduced NADPH-hemoprotein reductase] + O2
(7Z,10Z,13Z,19Z)-16,17-epoxydocosa-7,10,13,19-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosapentaenoic acid, 13,14-epoxydocosapentaenoic acid, and 10,11-epoxydocosapentaenoic acid, no formation of 21-hydroxy- or 22-hydroxydocosapentaenoic acid
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosapentaenoic acid, 13,14-epoxydocosapentaenoic acid, and 10,11-epoxydocosapentaenoic acid, no formation of 21-hydroxy- or 22-hydroxydocosapentaenoic acid
?
(7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoate + [reduced NADPH-hemoprotein reductase] + O2
(7Z,13Z,16Z,19Z)-10,11-epoxydocosa-7,13,16,19-tetraenoate + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosapentaenoic acid, 13,14-epoxydocosapentaenoic acid, and 10,11-epoxydocosapentaenoic acid, no formation of 21-hydroxy- or 22-hydroxydocosapentaenoic acid
Products: formation of 19,20-epoxydocosapentaenoic acid, 16,17-epoxydocosapentaenoic acid, 13,14-epoxydocosapentaenoic acid, and 10,11-epoxydocosapentaenoic acid, no formation of 21-hydroxy- or 22-hydroxydocosapentaenoic acid
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: hydroxylation at C-18
Products: hydroxylation at C-18
?
astemizole + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
luciferin 6'-2-(5-trifluoromethyl)furfuryl ether + [reduced NADPH-hemoprotein reductase] + O2
?
Substrates: -
Products: -
Products: -
?
luciferin 6'-2-fluorobenzyl ether + [reduced NADPH-hemoprotein reductase] + O2
?
Substrates: -
Products: -
Products: -
?
luciferin 6'-2-furfuryl ether + [reduced NADPH-hemoprotein reductase] + O2
?
Substrates: -
Products: -
Products: -
?
luciferin 6'-3-fluorobenzyl ether + [reduced NADPH-hemoprotein reductase] + O2
?
Substrates: -
Products: -
Products: -
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luciferin 6'-3-furfuryl ether + [reduced NADPH-hemoprotein reductase] + O2
?
Substrates: -
Products: -
Products: -
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luciferin 6'-3-thenylether + [reduced NADPH-hemoprotein reductase] + O2
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Substrates: -
Products: -
Products: -
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luciferin 6'-4-fluorobenzyl ether + [reduced NADPH-hemoprotein reductase] + O2
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Substrates: -
Products: -
Products: -
?
luciferin 6'-benzyl ether + [reduced NADPH-hemoprotein reductase] + O2
?
Substrates: -
Products: -
Products: -
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additional information
?
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Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
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Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
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Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
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Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
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Substrates: for all eight luciferin substrates, activity of enzyme CYP4Z1 is always highest, while that of enzyme CYP4F8 is always second highest, enzyme CYP4F12 is active only with luciferin 6'-benzyl ether, substrate binding modes, overview
Products: -
Products: -
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additional information
?
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Substrates: for all eight luciferin substrates, activity of enzyme CYP4Z1 is always highest, while that of enzyme CYP4F8 is always second highest, enzyme CYP4F12 is active only with luciferin 6'-benzyl ether, substrate binding modes, overview
Products: -
Products: -
?
additional information
?
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Substrates: for all eight luciferin substrates, activity of enzyme CYP4Z1 is always highest, while that of enzyme CYP4F8 is always second highest, enzyme CYP4F12 is active only with luciferin 6'-benzyl ether, substrate binding modes, overview
Products: -
Products: -
?
additional information
?
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Substrates: for all eight luciferin substrates, activity of enzyme CYP4Z1 is always highest, while that of enzyme CYP4F8 is always second highest, enzyme CYP4F12 is active only with luciferin 6'-benzyl ether, substrate binding modes, overview
Products: -
Products: -
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additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, luciferin 6'-2-furfuryl ether, luciferin 6'-3-furfuryl ether, and luciferin 6'-2-(5-trifluoromethyl)furfuryl ether
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, luciferin 6'-2-furfuryl ether, luciferin 6'-3-furfuryl ether, and luciferin 6'-2-(5-trifluoromethyl)furfuryl ether
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, luciferin 6'-2-furfuryl ether, luciferin 6'-3-furfuryl ether, and luciferin 6'-2-(5-trifluoromethyl)furfuryl ether
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, luciferin 6'-2-furfuryl ether, luciferin 6'-3-furfuryl ether, and luciferin 6'-2-(5-trifluoromethyl)furfuryl ether
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, and luciferin 6'-2-furfuryl ether, substrate binding modes, overview
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, and luciferin 6'-2-furfuryl ether, substrate binding modes, overview
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, and luciferin 6'-2-furfuryl ether, substrate binding modes, overview
Products: -
Products: -
?
additional information
?
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Substrates: no activity with luciferin 6'-2-fluorobenzyl ether, luciferin 6'-3-fluorobenzyl ether, luciferin 6'-4-fluorobenzyl ether, and luciferin 6'-2-furfuryl ether, substrate binding modes, overview
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
additional information
?
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Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme CYP4Z1 can catalyze the in-chain hydroxylation of lauric and myristic acid when expressed in Schizosaccharomyces pombe, and the CYP4Z1-dependent oxidation of arachidonic acid to its 14(S),15(R)-epoxide is observed
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
in the cytochrome P450 heme, catalytic heme iron
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isoforms CYP4F2/3, CYP4F11 and CYP4F12 vary 2.4- to 9.7fold, representing 36.4, 2.4 and 9.3% of total immunoquantified CYP1-4 proteins, respectively. CYP4F is the most abundant P450 subfamily in small intestines
brenda
additional information
isoforms CYP4F2/3, CYP4F11 and CYP4F12, vary 1.3- to 4.3fold, representing 8.0, 2.7 and 0.3% of total immunoquantified CYP1-4 proteins
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
outer surface of the plasma membrane
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
evolution
metabolism
physiological function
additional information
evolution
the enzyme CYP4F8 belongs to the cytochrome P450 (CYP) 4 family
evolution
the enzyme CYP4Z1 belongs to the cytochrome P450 (CYP) 4 family
evolution
the enzyme CYP4F12 belongs to the cytochrome P450 (CYP) 4 family
evolution
the enzyme CYP4F11 belongs to the cytochrome P450 (CYP) 4 family
metabolism
cytochrome P450 4F (CYP4F) isoforms are important phase I enzymes in the metabolism of many endogenous and exogenous substances. Cytochrome P450 4F (CYP4F) enzymes are responsible for the metabolism of eicosanoids, which play important roles in inflammation. Nuclear receptor liver X receptor alpha (LXRalpha) is a critical signal node connecting inflammation and lipid metabolism. The release of cytokines and nuclear factor-kappaB (NF-kappaB) can change the CYP4F11 expression in HepG2 cells. CYP4F11 is a target gene of LXRalpha. Regulation of CYP4F11 may contribute to the anti-inflammatory activity of LXRalpha agonists. LXRalpha agonists can reduce the transcriptional upregulation of inflammatory genes such as tumor necrosis factor-alpha (TNF-alpha) mediated by transcription factors such as NF-kappaB
metabolism
cytochrome P450 4F (CYP4F) isoforms are important phase I enzymes in the metabolism of many endogenous and exogenous substances. Cytochrome P450 4F (CYP4F) enzymes are responsible for the metabolism of eicosanoids, which play important roles in inflammation. Nuclear receptor liver X receptor alpha (LXRalpha) is a critical signal node connecting inflammation and lipid metabolism. The release of cytokines and nuclear factor-kappaB (NF-kappaB) can change the CYP4F11 transfection in mice. CYP4F40 is a target gene of LXRalpha. Regulation of CYP4F40 may contribute to the anti-inflammatory activity of LXRalpha agonists. LXRalpha agonists can reduce the transcriptional upregulation of inflammatory genes such as tumor necrosis factor-alpha (TNF-alpha) mediated by transcription factors such as NF-kappaB
physiological function
regulation of CYP4F11 may contribute to the anti-inflammatory activity of LXRalpha agonists
physiological function
regulation of CYP4F40 may contribute to the anti-inflammatory activity of LXRalpha agonists
additional information
synthesis of proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F8 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F8 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F8 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F8 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4Z1 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4Z1 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4Z1 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4Z1 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F12 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F12 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F12 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F12 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F11 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F11 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F11 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
additional information
synthesis of seven additional proluciferins for convenient activity determination of enzymes belonging to the cytochrome P450 (CYP) 4 family. Homology modeling of CYP4F11 using the X-ray structure of CYP4B1 (PDB ID 5TQ6) as template, structure-function analysis, detailed overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CP4F8_HUMAN
520
1
59995
Swiss-Prot
Secretory Pathway (Reliability: 2)
CP4Z1_HUMAN
505
2
59086
Swiss-Prot
Secretory Pathway (Reliability: 1)
CP4FC_HUMAN
524
2
60309
Swiss-Prot
Secretory Pathway (Reliability: 2)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G328E
mutant oxidizes prostaglandin H2 analogs U-51605 and U-44069 as recombinant CYP4F8, but the hydroxylation of arachidonic acid is shifted from C-18 to C-19
Y125F
missense mutation in substrate recognition site-1, occuring naturally in low frequency. The variant oxidizes prostaglandin H2 analogs U-51605, i.e. 9,11-diazo-prostadienoic acid, and U-44069, i.e. 9alpha,11alpha-epoxymethano-prostaglandin H2 in omega2 and omega3 position, but 4,7,10,13,16-(Z)-docosatetraenoic acid and 4,7,10,13,16-(Z)-docosapentaenoic acid are not oxidized
additional information
overexpression of CYP4F11 can decrease TNF-alpha and IL-1beta in lipopolysaccharide (LPS)-induced THP-1 cells
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CYP4F11, RT-PCR and quantitative real-time PCR enzyme expression analysis, recombinant overexpression of the enzyme in THP-1 cells
gene CYP4F12, recombinant expression in Schizosaccharomyces pombe
gene CYP4F40, RT-PCR and quantitative real-time PCR enzyme expression analysis, recombinant expression in transgenic mice
gene CYP4F8, recombinant expression in Schizosaccharomyces pombe
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GW3965 can activate LXRalpha, LXRalpha induces CYP4F11 promoter activity, positive regulation of cytochrome P450 4F11 expression by liver X receptor alpha (LXRalpha). LXRalpha increases the transcription of CYP4F11 and LXRalpha agonist GW3965 can induce the expression of CYP4F11 by activating the LXRalpha-CYP4F11 pathway
GW3965 can activate LXRalpha, LXRalpha induces CYP4F40 promoter activity, positive regulation of CYPP450 4F40 expression by liver X receptor alpha (LXRalpha). LXRalpha increases the transcription of CYP4F40 and LXRalpha agonist GW3965 can induce the expression of CYP4F40 by activating the LXRalpha-CYP4F40 pathway
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
missense mutation Y125F in substrate recognition site-1 occurs naturally in low frequency. The variant oxidizes two prostaglandin H2 analogs U-51605 and U-44069, but 4,7,10,13,16-(Z)-docosatetraenoic acid and 4,7,10,13,16-(Z)-docosapentaenoic acid are not oxidized
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stark, K.; Wongsud, B.; Burman, R.; Oliw, E.H.
Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8
Arch. Biochem. Biophys.
441
174-181
2005
Homo sapiens (P98187), Homo sapiens (Q9HCS2)
brenda
Uehara, S.; Murayama, N.; Nakanishi, Y.; Nakamura, C.; Hashizume, T.; Zeldin, D.C.; Yamazaki, H.; Uno, Y.
Immunochemical quantification of cynomolgus CYP2J2, CYP4A and CYP4F enzymes in liver and small intestine
Xenobiotica
45
124-130
2015
Macaca fascicularis (A8CBR8), Macaca fascicularis (A8CBS0)
brenda
Liu, J.; Machalz, D.; Wolber, G.; Sorensen, E.J.; Bureik, M.
New proluciferin substrates for human CYP4 family enzymes
Appl. Biochem. Biotechnol.
193
218-237
2021
Homo sapiens (P98187), Homo sapiens (Q9HCS2), Homo sapiens (Q86W10), Homo sapiens (Q9HBI6)
brenda
Zhang, T.; Zhan, Z.; Chen, Y.; Chen, J.; Han, W.; Liang, Z.; Liu, Q.; Liu, S.; Tang, L.
Regulation of cytochrome P450 4F11 expression by liver X receptor alpha
Int. Immunopharmacol.
90
107240
2021
Homo sapiens (Q9HBI6), Mus musculus (B2RY43)
brenda
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