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The biology of Mur ligases as an antibacterial target
Author(s) -
Kouidmi Imène,
Levesque Roger C.,
ParadisBleau Catherine
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12758
Subject(s) - biology , peptidoglycan , function (biology) , bacteria , antibacterial activity , biochemistry , computational biology , mechanism (biology) , enzyme , microbiology and biotechnology , genetics , philosophy , epistemology
Summary With antibiotic resistance mechanisms increasing in diversity and spreading among bacterial pathogens, the development of new classes of antibacterial agents against judiciously chosen targets is a high‐priority task. The biochemical pathway for peptidoglycan biosynthesis is one of the best sources of antibacterial targets. Within this pathway are the Mur ligases, described in this review as highly suitable targets for the development of new classes of antibacterial agents. The amide ligases MurC , MurD , MurE and MurF function with the same catalytic mechanism and share conserved amino acid regions and structural features that can conceivably be exploited for the design of inhibitors that simultaneously target more than one enzyme. This would provide multi‐target antibacterial weapons with minimized likelihood of target‐mediated resistance development.