doi: 10.1038/nsb0895-644.
An enzyme-substrate complex involved in bacterial cell wall biosynthesis
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- PMID: 7552726
- DOI: 10.1038/nsb0895-644
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An enzyme-substrate complex involved in bacterial cell wall biosynthesis
Nat Struct Biol.
1995 Aug.
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.
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