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An enzyme–substrate complex involved in bacterial cell wall biosynthesis

Nature Structural Biology volume 2, pages 644–653 (1995)Cite this article

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 Å 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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Authors and Affiliations

  1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts, 02115, USA

    Timothy E. Benson, David J. Filman, Christopher T. Walsh & James M. Hogle

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  4. James M. Hogle
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Benson, T., Filman, D., Walsh, C. et al. An enzyme–substrate complex involved in bacterial cell wall biosynthesis. Nat Struct Mol Biol 2, 644–653 (1995). https://doi.org/10.1038/nsb0895-644

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