Journal ArticleOPEN ACCESS

Biochemical properties of β-lactamase produced by Legionella gormanii

Antimicrobial Agents and Chemotherapy (1986) 29(5) 925-926
DOI: 10.1128/AAC.29.5.925
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Abstract

β-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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Fujii, T., Sato, K., Miyata, K., Inoue, M., & Mitsuhashi, S. (1986). Biochemical properties of β-lactamase produced by Legionella gormanii. Antimicrobial Agents and Chemotherapy, 29(5), 925–926. https://doi.org/10.1128/AAC.29.5.925

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