| Literature DB >> 12384342 |
Sophie Vimont1, Laurent Poirel, Thierry Naas, Patrice Nordmann.
Abstract
From whole-cell DNA of an enterobacterial Erwinia persicina reference strain that displayed a penicillinase-related antibiotic-resistant phenotype, a beta-lactamase gene was cloned and expressed in Escherichia coli. It encoded a clavulanic-acid-inhibited Ambler class A beta-lactamase, ERP-1, with a pI value of 8.1 and a relative molecular mass of ca. 28 kDa. ERP-1 shared 45 to 50% amino acid identity with the most closely related enzymes, the chromosomally encoded enzymes from Citrobacter koseri, Kluyvera ascorbata, Kluyvera cryocrescens, Klebsiella oxytoca, Proteus vulgaris, Proteus penneri, Rahnella aquatilis, Serratia fonticola, Yersinia enterocolitica, and the plasmid-mediated enzymes CTX-M-8 and CTX-M-9. The substrate profile of the noninducible ERP-1 was similar to that of these beta-lactamases. ERP-1 is the first extended-spectrum beta-lactamase from an enterobacterial species that is plant associated and plant pathogenic.Entities:
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Year: 2002 PMID： 12384342 PMCID： PMC128706 DOI： 10.1128/AAC.46.11.3401-3405.2002
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN： 0066-4804 Impact factor: 5.191