PMID:8631795

Citation	Brandish, PE, Burnham, MK, Lonsdale, JT, Southgate, R, Inukai, M and Bugg, TD (1996) Slow binding inhibition of phospho-N-acetylmuramyl-pentapeptide-translocase (Escherichia coli) by mureidomycin A. J. Biol. Chem. 271:7609-14
Abstract	Enzymes of the membrane cycle of reactions in bacterial peptidoglycan biosynthesis remain as unexploited potential targets for antibacterial agents. The first of these enzymes, phospho-N-acetylmuramyl-pentapeptide-translocase (EC 2.7.8.13), has been overexpresed in Escherichia coli and solubilized from particulate fractions. The work of W.A. Weppner and F.C. Neuhaus ((1977) J. Biol. Chem. 252, 2296-303) has been extended to establish a usable routine fluorescence-based continuous assay for solubilized preparations. This assay has been used in the characterization of the natural product, mureidomycin A as a potent slow binding inhibitor of the enzyme with Ki and Ki* of 36 nM and 2 nM, respectively.
Links	PubMed
Keywords	Anti-Bacterial Agents/pharmacology; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Fluorescent Dyes; Genetic Vectors; Isomerism; Kinetics; Models, Theoretical; Nucleosides/pharmacology; Plasmids; Recombinant Proteins/antagonists & inhibitors; Recombinant Proteins/biosynthesis; Recombinant Proteins/isolation & purification; Spectrometry, Fluorescence; Substrate Specificity; Transferases (Other Substituted Phosphate Groups)/antagonists & inhibitors; Transferases (Other Substituted Phosphate Groups)/biosynthesis; Transferases (Other Substituted Phosphate Groups)/isolation & purification
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