THE FOLDING OF SQUALENE - AN OLD PROBLEM HAS NEW RESULTS

被引:10
作者
BOHLMANN, R
机构
[1] Institut für Arzneimittelchemie der Schering AG, Berlin, D-W-1000
来源
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH | 1992年 / 31卷 / 05期
关键词
D O I
10.1002/anie.199205821
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
For the recognition of new applications of steroids, basic research is essential-especially when the desired effects are unprecedented in nature. In this context the recent reports by Corey et al. on the biogenesis of sterols is important. The enzyme sterolcyclase, which catalyzes the fourfold cyclization of the 2,3-epoxide-oxidosqualene (1) to lanosterol thus constructing the steroid framework in one step, can only now be purified. Once purified, the enzyme can be stored at 0-degrees-C for at least 14 days without loss of activity. Thus, further in-depth investigations into mechanistic aspects and the structure of the enzyme are now possible.
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页码:582 / 584
页数:3
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