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An enzyme-substrate complex involved in bacterial cell wall biosynthesis.

T E Benson·D J Filman·C T Walsh·J M Hogle
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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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Amino Acid SequenceAnti-Infective AgentsBinding SitesCarbohydrate DehydrogenasesCell WallComputer GraphicsComputer SimulationCrystallography, X-RayDrug DesignFlavin-Adenine DinucleotideHydrogen BondingLigandsModels, MolecularModels, StructuralMolecular Sequence DataPhosphoenolpyruvateProtein Structure, SecondaryUridine Diphosphate N-AcetylglucosamineUridine Diphosphate N-Acetylmuramic AcidJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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T E Benson, D J Filman, C T Walsh, J M Hogle. 1995. An enzyme-substrate complex involved in bacterial cell wall biosynthesis.. https://doi.org/10.1038/nsb0895-644

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