STERIC COURSE OF KETOPANTOATE HYDROXYMETHYLTRANSFERASE IN ESCHERICHIA-COLI

被引：22

作者：

ABERHART, DJ

RUSSELL, DJ

机构：

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 1984年 / 106卷 / 17期

关键词：

D O I：

10.1021/ja00329a045

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The conversion of .alpha.-ketoisovaleric acid (.alpha.-KIVA) to ketopantoate by the 5,10-methylenetetrahydrofolate-dependent enzyme ketopantoate hydroxymethyltransferase (KHMT) in E. coli was shown to proceed in a retention mode at the .beta.-position of .alpha.-KIVA. 5,10-Methylenetetrahydrofolate formed in vivo by serine hydroxymethyltransferase (SHMT) from stereospecifically deuterated (3S-d1) serine was converted by KHMT into an .apprx. 3:1 ratio of deuterated ketopantoates with the 4S isomer predominating. KHMT and SHMT apparently have the same overall steric course in E. coli.

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页码：4902 / 4906

页数：5

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