| Literature DB >> 22252797 |
Patrice Nordmann1, Anne E Boulanger, Laurent Poirel.
Abstract
A clinical Escherichia coli isolate resistant to all β-lactams, including carbapenems, expressed a novel metallo-β-lactamase (MBL), NDM-4, differing from NDM-1 by a single amino acid substitution (Met154Leu). NDM-4 possessed increased hydrolytic activity toward carbapenems and several cephalosporins compared to that of NDM-1. This amino acid substitution was not located in the known active sites of NDM-1, indicating that remote amino acid substitutions might also play a role in the extended activity of this MBL.Entities:
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Year: 2012 PMID: 22252797 PMCID: PMC3318389 DOI: 10.1128/AAC.05961-11
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191