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Information on EC 1.14.14.80 - long-chain fatty acid omega-monooxygenase and Organism(s) Rattus norvegicus and UniProt Accession P08516

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IUBMB Comments
A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (omega-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).
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Rattus norvegicus
UNIPROT: P08516
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyp4a1, cyp4a2, cyp4a3, cyp94c1, cyp4a8, cyp704b1, cyp52m1, cytochrome p450 4a11, cyp86a, cyp86a33, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP4A
CYP52M1
-
-
-
-
CYP704B1
-
-
-
-
CYP86A
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
long-chain fatty acid,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (omega-hydroxylating)
A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (omega-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
regioselectivity of omega:omega-1 hydroxylation is 6:1
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
regioselectivity of omega:omega-1 hydroxylation is 40:1
-
-
?
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
regioselectivity of omega:omega-1 hydroxylation is 3:1
-
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
regioselectivity of omega:omega-1 hydroxylation is 1:1
-
-
?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
myristic acid + [reduced NADPH-hemoprotein reductase] + O2
14-hydroxymyristic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
18-hydroxyoleic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
16-hydroxypalmitic acid + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
lauric acid
pH 7.4, 37°C
0.046
myristic acid
pH 7.4, 37°C
0.003 - 0.019
arachidonic acid
0.03 - 0.08
lauric acid
0.004 - 0.013
myristic acid
0.018 - 0.064
oleic acid
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
arachidonic acid
pH 7.4, 37°C
10.8
lauric acid
pH 7.4, 37°C
3.8
myristic acid
pH 7.4, 37°C
0.02
oleic acid
pH 7.4, 37°C
1
palmitic acid
pH 7.4, 37°C
0.02 - 0.03
arachidonic acid
0.58 - 3.8
lauric acid
0.1 - 1.17
myristic acid
0.01 - 0.02
oleic acid
0.03 - 0.1
palmitic acid
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultured hepatocyte
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
omega-hydroxylated eicosatrienoic acids may serve as endogenous peroxisome proliferator-activated receptor alpha ligands. P450 arachidonic acid monooxygenases such as CYP2C epoxygenase and CYP4A omega-hydroxylase participate in ciprofibrate-induced peroxisomal proliferation and the activation of peroxisome proliferator-activated receptor alpha downstream targets
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP4AA_RAT
509
2
58215
Swiss-Prot
Secretory Pathway (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in ciprofibrate-treated cells, CYP4A expression increases by 1.5- to 1.8fold
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
specific inhibition of either the CYP2C epoxygenase or the CYP4A omega-hydroxylase abrogates peroxisomal proliferation induced by the hypolipidemic drug cirpofibrate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoch, U.; Zhang, Z.; Kroetz, D.L.; Ortiz de Montellano, P.R.
Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid omega-hydroxylases
Arch. Biochem. Biophys.
373
63-71
2000
Homo sapiens (Q02928), Homo sapiens, Rattus norvegicus (P08516), Rattus norvegicus (P20816), Rattus norvegicus (P20817), Rattus norvegicus (P24464)
Manually annotated by BRENDA team
Gatica, A.; Aguilera, M.C.; Contador, D.; Loyola, G.; Pinto, C.O.; Amigo, L.; Tichauer, J.E.; Zanlungo, S.; Bronfman, M.
P450 CYP2C epoxygenase and CYP4A omega-hydroxylase mediate ciprofibrate-induced PPARalpha-dependent peroxisomal proliferation
J. Lipid Res.
48
924-934
2007
Rattus norvegicus
Manually annotated by BRENDA team