Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
- 15 September 1996
- Vol. 4 (9) , 1065-1075
- https://doi.org/10.1016/s0969-2126(96)00113-x
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- The herbicide glyphosate is a potent inhibitor of 5-enolpyruvylshikimic acid-3-phosphate synthasePublished by Elsevier ,2004
- The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesisChemistry & Biology, 1996
- The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell wallsStructure, 1996
- An enzyme–substrate complex involved in bacterial cell wall biosynthesisNature Structural & Molecular Biology, 1995
- Kinetics, Stoichiometry, and Identification of the Reactive Thiolate in the Inactivation of UDP-GlcNAc Enolpyruvoyl Transferase by the Antibiotic FosfomycinBiochemistry, 1994
- Evidence that the reaction of the UDP‐N‐acetylglucosamine 1‐carboxyvinyltransferase proceeds through the O‐phosphothioketal of pyruvic acid bound to Cys115 of the enzymeEuropean Journal of Biochemistry, 1993
- The UDP‐N‐acetylglucosamine 1‐carboxyvinyl‐transferase of Enterobacter cloacae Molecular cloning, sequencing of the gene and overexpression of the enzymeFEBS Letters, 1992
- Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: enzymology, antibiotics, and antibiotic resistanceNatural Product Reports, 1992
- Kinetic and structural analysis of enzyme intermediates: lessons from EPSP synthaseChemical Reviews, 1990
- THE MECHANISM OF ACTION OF FOSFOMYCIN (PHOSPHONOMYCIN)Annals of the New York Academy of Sciences, 1974