| Literature DB >> 7552726 |
T E Benson1, D J Filman, C T Walsh, J M Hogle.
Abstract
The crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase in the presence of its substrate, enolpyruvyl-UDP-N-acetylglucosamine, has been solved to 2.7 A 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.Entities:
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Year: 1995 PMID： 7552726 DOI： 10.1038/nsb0895-644
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368