DIFFERENT SUBSTRATE SPECIFICITIES OF LANOSTEROL 14-ALPHA-DEMETHYLASE (P-45014DM) OF SACCHAROMYCES-CEREVISIAE AND RAT-LIVER FOR 24-METHYLENE-24,25-DIHYDROLANOSTEROL AND 24,25-DIHYDROLANOSTEROL

被引：36

作者：

AOYAMA, Y

YOSHIDA, Y

机构：

[1] Faculty of Pharmaceutical Sciences, Mukogawa Women's University 11-68 Koshien-Kyubancho, Nishinomiya

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 178卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)91000-3

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 purified lanosterol 14α-demethylase (P-45014DM) of S. cerevisiae catalyzed the 14α-demethylation of 24-methylene-24,25-dihydrolanosterol (24-methylenelanost-8-en-3β-ol, 24-methylene-DHL), the natural substrate of the demethylase of filamentous fungi, as well as its natural substrate, lanosterol. Lanosterol 14α-demethylase of rat liver microsomes also catalyzed the 14α-demethylation of 24-methylene-DHL, but the activity was considerably lower than that for lanosterol. The activity of the rat liver enzyme for 24-methylene-DHL was also lower than that for 24,25-dihydrolanosterol (DHL), while the activity of yeast P-45014DM for 24-methylene-DHL was considerably higher than that for DHL. Since 24-substituted sterols are not found in mammals and DHL is not an intermediate of ergosterol biosynthesis by yeast, above-mentioned different substrate specificities between the yeast and the mammalian 14α-demethylases may reflect certain evolutional alteration in their active sites in relation to the difference in their sterol biosynthetic pathways. © 1991.

引用

页码：1064 / 1071

页数：8

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