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pubmed:abstractText |
From whole-cell DNA of a clinical isolate of the enterobacterial species Rahnella aquatilis, a beta-lactamase gene was cloned that encoded a chromosomally encoded Ambler class A enzyme, RAHN-1. RAHN-1, with a pI of 7.2, shares 76, 73, and 71% amino acid identity with the extended-spectrum beta-lactamase of chromosomal origin from Serratia fonticola and with the plasmid-mediated beta-lactamases CTX-M-2 and CTX-M-1, respectively. The hydrolysis spectrum of the clavulanic acid-inhibited RAHN-1 was expanded to cephalosporins such as cefuroxime, cefotaxime, and ceftriaxone, but not to ceftazidime. Its expression was not inducible.
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pubmed:affiliation |
Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, 78 rue de Général Leclerc, 94275 Le Kremlin-Bicêtre Cedex, France.
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