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FEMS Microbiol Lett. 1996 Sep 15;143(1):29-33.

A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins.

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1
Service de Bactériologie-Virologie, Hôpital Lariboisière, Paris, France.

Abstract

In order to analyze its kinetic parameters, an Ambler class A carbapenemase NMC-A was purified. NMC-A demonstrated unusually strong hydrolytic activity towards imipenem and meropenem. Moreover, it hydrolyzed cephamycins with kcat values uncommonly high for this class of beta-lactamases. Clavulanic acid and tazobactam had comparable inhibitory activity against NMC-A, whereas sulbactam was the least active inhibitor. Noticeably, NMC-A was more readily inhibited by brobactam. All these catalytic properties suggest that NMC-A possesses an original structure of its active site allowing hydrolysis of beta-lactams usually stable to the hydrolytic activity of class A beta-lactamases.

[Indexed for MEDLINE]

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