Primary citation
Title 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,; Mistry,; Wonacott,; Hutchinson,; Kelly,; Duncan,
Journal STRUCTUREsearch vol:4, pag:1465-1474 (1996), Identifiers: PubMed ID (8994972)search DOI (10.1016/S0969-2126(96)00153-0)
Abstract UDP-N-acetylglucosamine enolpyruvyl transferase (MurA), catalyses the first committed step of bacterial cell wall biosynthesis and is a target for the antibiotic fosfomycin. The only other known enolpyruvyl transferase is 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase, an enzyme involved in the shikimic acid pathway and the target for the herbicide glyphosate. Inhibitors of enolpyruvyl transferases are of biotechnological interest as MurA and EPSP synthase are found exclusively in plants and microbes.
MeSH terms 3-Phosphoshikimate 1-Carboxyvinyltransferasesearch, Alkyl and Aryl Transferasessearch, Anti-Bacterial Agentssearch, Bacterial Proteinssearch, Binding Sitessearch, Cell Wallsearch, Crystallographysearch, X-Raysearch, Escherichia colisearch, Fosfomycinsearch, Hydrogen Bondingsearch, Modelssearch, Molecularsearch, Peptidoglycansearch, Protein Bindingsearch, Protein Conformationsearch, Protein Structuresearch, Tertiarysearch, Transferasessearch, Uridine Diphosphate N-Acetylglucosaminesearch
Secondary citations
Title Cloning and Sequencing of Escherichia Coli Murz and Purification of its Product, a Udp-N-Acetylglucosamine Enolpyruvyl Transferase
Authors Marquardt,; Siegele,; Kolter,; Walsh,
Journal vol:174, pag:5748 (1992)