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. 1986 May;29(5):925-6.
doi: 10.1128/AAC.29.5.925.

Biochemical properties of beta-lactamase produced by Legionella gormanii

T Fujii, K Sato, K Miyata, M Inoue, S Mitsuhashi

Biochemical properties of beta-lactamase produced by Legionella gormanii

T Fujii et al. Antimicrob Agents Chemother. 1986 May.

Abstract

beta-Lactamase was purified from a strain of Legionella gormanii. The molecular weight of the purified enzyme was 25,000, and its isoelectric point was 10.5. The enzyme hydrolyzed oxyiminocephalosporins, cephamycins, penicillins, and imipenem. The enzyme activity was inhibited by EDTA, Hg2+, and Cu2+, but not by clavulanic acid, sulbactam, or imipenem.

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