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NDM-4 metallo-?-lactamase with increased carbapenemase activity from Escherichia coli.

ABSTRACT: A clinical Escherichia coli isolate resistant to all ?-lactams, including carbapenems, expressed a novel metallo-?-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.

SUBMITTER: Nordmann P 

PROVIDER: S-EPMC3318389 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

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NDM-4 metallo-β-lactamase with increased carbapenemase activity from Escherichia coli.

Nordmann Patrice P   Boulanger Anne E AE   Poirel Laurent L  

Antimicrobial agents and chemotherapy 20120117 4

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 acti  ...[more]

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