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. 2001 Dec;45(12):3595-8.
doi: 10.1128/AAC.45.12.3595-3598.2001.

Characterization of a chromosomally encoded extended-spectrum class A beta-lactamase from Kluyvera cryocrescens

J W Decousser  1 , L Poirel, P Nordmann
Affiliations

Characterization of a chromosomally encoded extended-spectrum class A beta-lactamase from Kluyvera cryocrescens

J W Decousser et al. Antimicrob Agents Chemother. 2001 Dec.

Abstract

A chromosomally located beta-lactamase gene, cloned and expressed in Escherichia coli from a reference strain of the enterobacterial species Kluyvera cryocrescens, encoded a clavulanic acid-inhibited Ambler class A enzyme, KLUC-1, with a pI value of 7.4. KLUC-1 shared 86% amino acid identity with a subgroup of plasmid-mediated CTX-M-type extended-spectrum beta-lactamases (CTX-M-1, -3, -10, -11, and -12), the most closely related enzymes, and 77% amino acid identity with KLUA-1 from Kluyvera ascorbata. The substrate profile of KLUC-1 corresponded to that of CTX-M-type enzymes.

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Figures

FIG. 1
FIG. 1
Alignment of the KLUC-1 amino acid sequence with those of CTX-M-10 from E. coli (31), KLUA-1 from K. ascorbata (GenBank accession no. CAB 59824), Toho-1 from E. coli (14), CTX-M-9 from E. coli (27), and CTX-M-8 from Enterobacter cloacae (7). The numbering is according to Ambler et al. (2). Dashes indicate identical amino acid residues. The vertical arrow indicates the putative cleavage site of the leader peptide of the mature KLUC-1 β-lactamase. Four structural elements characteristic of class A β-lactamases are shaded (17). The amino acids of the omega loop are underlined.
See this image and copyright information in PMC

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