| Literature DB >> 27021004 |
Timothy D H Bugg1, Maria T Rodolis2, Agnes Mihalyi2, Shirin Jamshidi2.
Abstract
This review covers recent developments in the inhibition of translocase MraY and related phospho-GlcNAc transferases WecA and TagO, and insight into the inhibition and catalytic mechanism of this class of integral membrane proteins from the structure of Aquifex aeolicus MraY. Recent studies have also identified a protein-protein interaction site in Escherichia coli MraY, that is targeted by bacteriophage ϕX174 lysis protein E, and also by cationic antimicrobial peptides containing Arg-Trp close to their N- or C-termini. Copyright ÂEntities:
Keywords: Bacteriophage lysis protein E; Cationic antimicrobial peptides; Enzyme inhibition; Nucleoside antibiotics; Peptidoglycan biosynthesis; Translocase MraY
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Year: 2016 PMID: 27021004 DOI: 10.1016/j.bmc.2016.03.018
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641