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10.1021/cb4001603 http://scihub22266oqcxt.onion/10.1021/cb4001603 C4013547!4013547!23574509     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=23574509&cmd=llinks): Failed to open stream: HTTP request failed! 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The structure of Enterococcus Faeciuml,d?transpeptidase acylated by ertapenem provides insight into the inactivation mechanism |pdf=|usr=}}{{23574509}} gab.com Text The structure of Enterococcus Faeciuml,d transpeptidase acylated by ertapenem provides insight into the inactivation mechanism JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=23574509 #FOAvip The maintenance of bacterial cell shape and integrity is largely attributed to peptidoglycan, a biopolymer highly cross-linked through d,d?transpeptidation. Peptidoglycan cross-linking is catalyzed by Penicillin-Binding Proteins (PBPs) that are the essential target of ?-lactam antibiotics. PBPs are functionally replaced by l,d?transpeptidases (Ldts) in ampicillin? resistant mutants of Enterococcus faecium and in wild-type Mycobacterium tuberculosis. Ldts are inhibited in vivo by a single class of ?-lactams, the carbapenems, which act as a suicide substrate. We present here the first structure of a carbapenem?acylated l,d?transpeptidase, E. faecium Ldtfm acylated by ertapenem, which revealed key contacts between the carbapenem core and residues of the catalytic cavity of the enzyme. Significant reorganization of the antibiotic conformation occurs upon enzyme acylation. These results, together with the analysis of protein?to?carbapenem proton transfers, provide new insight into the mechanism of Ldt acylation by carbapenems. Twit Text FOAVip The structure of Enterococcus Faeciuml,d transpeptidase acylated by ertapenem provides insight into the inactivation mechanism ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=23574509 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23574509 #FOAvip English Wikipedia <ref>{{Cite pmid|23574509}}</ref> The structure of Enterococcus Faeciuml,d?transpeptidase acylated by ertapenem provides insight into the inactivation mechanism #MMPMID23574509 Lecoq L; Dubée V; Triboulet S; Bougault C; Hugonnet JE; Arthur M; Simorre JP ACS Chem Biol 2013[]; 8 (6): 1140-6 PMID23574509show ga The maintenance of bacterial cell shape and integrity is largely attributed to peptidoglycan, a biopolymer highly cross-linked through d,d?transpeptidation. Peptidoglycan cross-linking is catalyzed by Penicillin-Binding Proteins (PBPs) that are the essential target of ?-lactam antibiotics. PBPs are functionally replaced by l,d?transpeptidases (Ldts) in ampicillin? resistant mutants of Enterococcus faecium and in wild-type Mycobacterium tuberculosis. Ldts are inhibited in vivo by a single class of ?-lactams, the carbapenems, which act as a suicide substrate. We present here the first structure of a carbapenem?acylated l,d?transpeptidase, E. faecium Ldtfm acylated by ertapenem, which revealed key contacts between the carbapenem core and residues of the catalytic cavity of the enzyme. Significant reorganization of the antibiotic conformation occurs upon enzyme acylation. These results, together with the analysis of protein?to?carbapenem proton transfers, provide new insight into the mechanism of Ldt acylation by carbapenems. äThe structure of Enterococcus Faeciuml,d?transpeptidase acylated by er(epmc).pdf DeepDyve Pubget Overpricing