| Literature DB >> 1901695 |
M Watanabe1, S Iyobe, M Inoue, S Mitsuhashi.
Abstract
We isolated an imipenem-resistant strain, GN17203, of Pseudomonas aeruginosa. The strain produced a beta-lactamase that hydrolyzed imipenem. The beta-lactamase was encoded by a 31-MDa plasmid, pMS350, which belongs to incompatibility group P-9. The plasmic conferred resistance to beta-lactams, gentamicin, and sulfonamide and was transferable by conjugation to P. aeruginosa but not to Escherichia coli. The molecular weight of the purified enzyme was estimated to be 28,000, and the isoelectric point was 9.0. The enzyme showed a broad substrate profile, hydrolyzing imipenem, oxyiminocephalosporins, 7-methoxycephalosporins, and penicillins. The enzyme activity was inhibited by EDTA, iodine, p-chloromercuribenzoate, CuSO4, and HgCl2 but not by clavulanic acid or sulbactam.Entities:
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Year: 1991 PMID: 1901695 PMCID: PMC244956 DOI: 10.1128/AAC.35.1.147
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191