| Literature DB >> 16189095 |
Claire Héritier1, Laurent Poirel, Pierre-Edouard Fournier, Jean-Michel Claverie, Didier Raoult, Patrice Nordmann.
Abstract
A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. beta-Lactamase OXA-69 shared 97% amino acid identity with the recently described OXA-51 enzyme of A. baumannii and 62 and 56% amino acid identity with the carbapenem-hydrolyzing oxacillinases OXA-24 and OXA-23, respectively. Biochemical characterization of the purified OXA-69 revealed a narrow-spectrum hydrolysis profile but including, at a low level, imipenem and meropenem. By PCR and sequencing bla(OXA-69)-like genes were identified in all A. baumannii strains tested (n = 12), suggesting that this oxacillinase is naturally occurring in that species.Entities:
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Year: 2005 PMID: 16189095 PMCID: PMC1251506 DOI: 10.1128/AAC.49.10.4174-4179.2005
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191