OXIDATION OF 5-BETA-CHOLESTANE-3-ALPHA,7-ALPHA,12-ALPHA-TRIOL INTO 3-ALPHA,7-ALPHA,12-ALPHA-TRIHYDROXY-5-BETA-CHOLESTANOIC ACID BY CYTOCHROME-P-45026 FROM RABBIT LIVER-MITOCHONDRIA

被引：18

作者：

DAHLBACK, H

HOLMBERG, I

机构：

[1] Department of Pharmaceutical Biochemistry, University of Uppsala, S-751 23 Uppsala

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92034-W

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The mitochondrial cytochrome P-45026, previously shown to catalyze 26-hydroxylation of 5β-cholestane-3α,7α,12α-triol, was found to convert this substrate also into 3α,7α,12α-trihydroxy-5β-cholestanoic acid. The formation of 3α,7α,12α-trihydroxy-5β-cholestanoic acid increased with increasing incubation time and enzyme concentration. Addition of NAD+ to the incubation mixture did not increase the formation of the acid. Incubation with 5β-cholestane-3α,7α,12α,26-tetrol, cytochrome P-45026, ferredoxin, ferredoxin reductase and NADPH resulted in one major product, 3α,7α,12α-trihydroxy-5β-cholestanoic acid. The cytochrome P-450 required both ferredoxin, ferredoxin reductase and NADPH for activity. NADPH could not be replaced by NAD+ or NADP+. © 1990.

引用

页码：391 / 395

页数：5

共 24 条

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