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Essential residues for the enzyme activity of ATP-dependent murE ligase from mycobacterium tuberculosis

Protein & Cell 2010年第11期1卷 1011-1022页

作者： Chandrakala Basavannacharya Paul R.moody Tulika munshi Nora Cronin Nicholas H.Keep Sanjib Bhakta Institute for Structural and molecular Biology Department of Biological SciencesBirkbeckUniversity of LondonLondon WC1E 7HXUK

The emergence of total drug-resistant tuberculosis(TDRTB)has made the discovery of new therapies for tuberculosis *** cytoplasmic enzymes of peptidoglycan biosynthesis have generated renewed interest as attractive targets for the development of new *** of the cytoplasmic enzymes,uridine diphosphate(UDP)-murNAc-tripeptide ligase(murE),catalyses the addition of meso-diaminopimelic acid(m-dap)into peptidoglycan in mycobacterium tuberculosis coupled to the hydrolysis of *** of *** murE were generated by replacing K157,E220,D392,R451 with alanine and N449 with aspartate,and truncating the first 24 amino acid residues at the Nterminus of the *** of the specific activity of these proteins suggested that apart from the 24 Nterminal residues,the other mutated residues are essential for *** in Km values for one or more substrates were observed for all mutants,except the N-terminal truncation mutant,indicating that these residues are involved in binding substrates and form part of the active site *** mutant proteins were also tested for their specificity for a wide range of ***,the mutations K157A,E220A and D392A showed hydrolysis of ATP uncoupled from *** ATP hydrolysis rate was enhanced by at least partial occupation of the uridine nucleotide dipeptide binding *** study provides an insight into the residues essential for the catalytic activity and substrate binding of the ATP-dependent murE *** ATPdependent murE ligase is a novel drug target,the understanding of its function may lead to development of novel inhibitors against resistant forms of ***.

关键词： peptidoglycan murE ligase site-directed mutagenesis m-dap

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