Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis

被引：80

作者：

Born, TL ^{[1
]}

Blanchard, JS ^{[1
]}

机构：

[1] Yeshiva Univ Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1999年 / 3卷 / 05期

关键词：

D O I：

10.1016/S1367-5931(99)00016-2

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：

Within the past 18 months work has continued on the structure and mechanisms of enzymes involved in the diaminopimelic acid/lysine biosynthetic pathway. A novel structure has been determined for a PLP-independent epimerase, and structures with bound substrates have been solved for two other enzymes. Additionally, new studies have appeared describing the chemical mechanisms of three enzymes in the pathway.

引用

页码：607 / 613

页数：7

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