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Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin.

Authors
  • Skarzynski, T
  • Mistry, A
  • Wonacott, A
  • Hutchinson, S E
  • Kelly, V A
  • Duncan, K
Type
Published Article
Journal
Structure
Publisher
Elsevier BV
Publication Date
Dec 15, 1996
Volume
4
Issue
12
Pages
1465–1474
Identifiers
PMID: 8994972
Source
Medline
License
Unknown

Abstract

The present structure reveals the mode of binding of the natural substrate UDP-GlcNAc and of the drug fosfomycin, and provides information on the residues involved in catalysis. These results should aid the design of inhibitors which would interfere with enzyme-catalyzed reactions in the early stage of the bacterial cell wall biosynthesis. Furthermore, the crystal structure of MurA provides a model for predicting active-site residues in EPSP synthase that may be involved in catalysis and substrate binding.

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