UNIQUE PROPERTY OF LIVER MITOCHONDRIAL-P450 TO CATALYZE THE 2 PHYSIOLOGICALLY IMPORTANT REACTIONS INVOLVED IN BOTH CHOLESTEROL CATABOLISM AND VITAMIN-D ACTIVATION

被引：43

作者：

USUI, E

NOSHIRO, M

OHYAMA, Y

OKUDA, K

机构：

[1] Department of Biochemistry, Hiroshima University School of Dentistry. Hiroshima

来源：

FEBS LETTERS | 1990年 / 274卷 / 1-2期

关键词：

12α-triol; 7α; Vitamin D 25-hydroxylase: Cytochrome P450: 5β-Cholestane-3α;

D O I：

10.1016/0014-5793(90)81357-T

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 cDNA for vitamin D 25-hydroxylase in rat liver mitochondria was transfected in COS cells in order to confirm our previous postulation that both 5β-cholestane-3α,7α,12α-triol 27-hydroxylation and vitamin D 25-hydroxylation are catalyzed by a common enzyme. As a result it was found that both enzyme activities could be reconstituted from the solubilized extract of mitochondria of these cells. NADPH. NADPH-adrenodoxin reductase and adrenodoxin, giving unequivocal evidence that the two enzyme activities are catalyzed by a common enzyme. © 1990.

引用

页码：175 / 177

页数：3

共 26 条

[1]

ANDERSSON S, 1989, J BIOL CHEM, V264, P8222

[2] OMEGA-HYDROXYLASE FOR 5BETA-CHOLESTANE-3ALPHA,7 ALPHA-DIOL IN BIOSYNTHESIS OF CHENODEOXYCHOLIC ACID [J].