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Int J Antimicrob Agents. 2007 Feb;29(2):159-64. Epub 2007 Jan 4.

Biochemical characterisation of the CTX-M-14 beta-lactamase.

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1
Centre for Protein Engineering, University of Liège, B6 Institute of Chemistry, Sart Tilman, B4000 Liège, Belgium. yoishii@med.toho-u.ac.jp

Abstract

Cefotaxime-resistant Escherichia coli TUM1121 was isolated from an abscess of an 83-year-old patient. The CTX-M-14 gene was located on a 70 kb plasmid. The enzyme was purified and its activity was analysed. CTX-M-14 was poorly active against ceftazidime and aztreonam. Aztreonam behaved as a competitive inhibitor. Among the tested suicide substrates for class A beta-lactamases, sulbactam was a rather good substrate. Tazobactam and clavulanic acid behaved as inactivators. The interactions between clavulanic acid and CTX-M-14 were characterised by progressive inactivation of the beta-lactamase. Carbapenems such as imipenem, meropenem or doripenem did not behave as inactivators of CTX-M-14, however very small k(cat) values were observed. This result shows that CTX-M-14 is able to hydrolyse carbapenems.

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