AN ENZYME-SUBSTRATE COMPLEX INVOLVED IN BACTERIAL-CELL WALL BIOSYNTHESIS

被引：81

作者：

BENSON, TE ^{[1
]}

FILMAN, DJ ^{[1
]}

WALSH, CT ^{[1
]}

HOGLE, JM ^{[1
]}

机构：

[1] HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL,BOSTON,MA 02115

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 08期

关键词：

D O I：

10.1038/nsb0895-644

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 crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase in the presence of its substrate, enolpyruvyl-UDP-N-acetylglucosamine, has been solved to 2.7 Angstrom resolution. This enzyme is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis and consequently provides an attractive target for the design of antibacterial agents. The structure reveals a novel flavin binding motif, shows a striking alignment of the flavin with the substrate, and suggests a catalytic mechanism for the reduction of this unusual enol ether.

引用

页码：644 / 653

页数：10

共 47 条

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