Title : Omega- and (omega-1)-hydroxylation of arachidonic acid, lauric acid and prostaglandin A1 by multiple forms of cytochrome P-450 purified from rat hepatic microsomes.

Pub. Date : 1990 Apr 2

PMID : 2317528






3 Functional Relationships(s)
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Protein Name
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1 In a reconstituted system with purified cytochromes P-450, P450 UT-1, UT-2 (P-450h), MC-1 (P-450d) and MC-5 (P-450c) effectively hydroxylated arachidonic acid at both the omega- and (omega-1)-position. Arachidonic Acid cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus
2 Lauric acid was also hydroxylated by P450 UT-1, UT-2, PB-1, PB-2, MC-1, IF-3 (P-450a) and DM, at the (omega - 1)-position only. lauric acid cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus
3 P450 UT-2 and PB-1 could hydroxylate prostaglandin A1 by (omega-1)-hydroxylation, but with low activity. prostaglandin A1 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus