PREFERENTIAL CYCLIZATION OF 2,3(S)/22(S),23-DIOXIDOSQUALENE BY MAMMALIAN 2,3-OXIDOSQUALENE-LANOSTEROL CYCLASE

被引：33

作者：

BOUTAUD, O ^{[1
]}

DOLIS, D ^{[1
]}

SCHUBER, F ^{[1
]}

机构：

[1] FAC PHARM ILLKIRCH,CHIM BIOORGAN LAB,CNRS,URA 1386,74 ROUTE RHIN,F-67400 ILLKIRCH GRAFFENS,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 188卷 / 02期

关键词：

D O I：

10.1016/0006-291X(92)91140-L

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：

Kinetic studies on the cyclization of 2,3(S)-oxido and 2,3(S):22(S),23-dioxido[14C]squa-lene catalyzed by liver oxidosqualene-lanosterol cyclase revealed a specificity (in terms of V /Km) of the enzyme for the diepoxide. The specificity ratio was dependent on the enzyme preparation, i.e. purified or microsomal, and was highest (about 5) with the microsomal enzyme m the presence of supernatant protein factors. These results explain why, in the presence of cyclase inhibitors, the squalene epoxides can be channeled into a cholesterol biosynthesis regulatory pathway via 24(S),25-epoxylanosterol and 24(S),25-epoxycholesterol. © 1992.

引用

页码：898 / 904

页数：7

共 19 条

[1]

CARAS IW, 1979, J BIOL CHEM, V254, P1816

[2]

CATTEL L, 1989, Steroids, V53, P363, DOI 10.1016/0039-128X(89)90020-2

[3]

CHANG TY, 1979, J BIOL CHEM, V254, P1258

[4]

CHIN J, 1984, J BIOL CHEM, V259, P1735