View source for PMID:16377691

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!align=left  |Citation
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'''Baum, EZ, Crespo-Carbone, SM, Abbanat, D, Foleno, B, Maden, A, Goldschmidt, R and Bush, K'''  (2006) Utility of muropeptide ligase for identification of inhibitors of the cell wall biosynthesis enzyme MurF. ''Antimicrob. Agents Chemother.'' '''50''':230-6
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!align=left  |Abstract
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MurF is a key enzyme in the biosynthesis of the bacterial cell wall in both gram-positive and gram-negative bacteria. This enzyme has not been extensively exploited as a drug target, possibly due to the difficulty in obtaining one of the substrates, UDP-MurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate, which is usually purified from bacteria. We have identified putative inhibitors of Escherichia coli MurF by a binding assay, thus bypassing the need for substrate. Inhibition of enzymatic activity was demonstrated in a high-performance liquid chromatography-based secondary assay with UDP-MurNAc-L-Ala-gamma-D-Glu-diaminopimelate substrate prepared in a novel way by using muropeptide ligase enzyme to add UDP-MurNAc to synthetic L-Ala-gamma-D-Glu-diaminopimelate; the substrate specificity of muropeptide ligase for peptides containing L-Lys in place of diaminopimelate was also investigated. Using the muropeptide ligase-generated MurF substrate, a thiazolylaminopyrimidine series of MurF enzyme inhibitors with 50% inhibitory concentration values as low as 2.5 microM was identified.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16377691 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1346814 PMC1346814]
Online version:[http://dx.doi.org/10.1128/AAC.50.1.230-236.2006 10.1128/AAC.50.1.230-236.2006]
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!align=left  |Keywords
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Cell Wall/metabolism; Enzyme Inhibitors/isolation & purification; Enzyme Inhibitors/pharmacology; Escherichia coli/chemistry; Escherichia coli/enzymology; Peptide Synthases/antagonists & inhibitors; Peptide Synthases/metabolism; Peptidoglycan/biosynthesis

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