1887

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Volume 58, Issue 6

Characterization of two plasmid-encoded cefotaximases found in clinical isolates: CTX-M-65 and a novel enzyme, CTX-M-87 Free

Abstract

Three clinical strains of (p168, p517 and p667) were collected in 2006 from three hospitals in Anhui Province (China). PCR and DNA sequencing revealed that p168 carried a novel extended-spectrum -lactamase (ESBL), which was designated CTX-M-87. The extended-spectrum -lactamase which was carried by p517 and p667 was previously named CTX-M-65. The deduced amino acid sequence of CTX-M-87, with pI 9.1, differed from that of CTX-M-14 by the substitutions Ala77→Val and Pro167→Leu. Like CTX-M-14, CTX-M-87 had a more potent hydrolytic activity against cefotaxime than against ceftazidime and had high affinity for cefuroxime and cefotaxime. These data show that mutations at position 167 in CTX-M do not always affect catalytic activity and substrate preference.

  • Received:
  • Accepted:
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Keyword(s): ESBL, extended-spectrum β-lactamase
SGM
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2009-06-01
2024-05-02
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Characterization of two plasmid-encoded cefotaximases found in clinical Escherichia coli isolates: CTX-M-65 and a novel enzyme, CTX-M-87
J. Med. Microbiol. 58, 811 (2009); https://doi.org/10.1099/jmm.0.006007-0
/content/journal/jmm/10.1099/jmm.0.006007-0
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