Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme.
作者： S Andersson , D L Davis , H Dahlbäck , H Jörnvall , D W Russell
DOI: 10.1016/S0021-9258(18)83172-6
关键词:
摘要: The conversion of cholesterol into bile acids in the liver represents major catabolic pathway for removal from body. In this complex biosynthetic pathway, at least 10 enzymes modify both ring structure and side chain cholesterol, resulting formation primary acids, cholic acid, chenodeoxycholic acid. To gain insight details regulation we have used protein sequencing molecular cloning techniques to isolate characterize a cDNA encoding rabbit mitochondrial sterol 26-hydroxylase. This enzyme catalyzes first step oxidation intermediates biosynthesis acids. 26-hydroxylase, as deduced by DNA sequence analysis analysis, reveals it be cytochrome P-450. A signal 36 residues precedes coding region 499 amino predicting weight 56,657 mature protein. identity 26-hydroxylase was further confirmed expression monkey COS cells employing versatile eukaryotic vector. Blotting experiments revealed that mRNA is expressed many tissues encoded low copy number gene genome.
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