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.
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页码：644 / 653
页数：10
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