title: Biochemical properties of beta-lactamase produced by Legionella gormanii.
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.
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D007525:Isoelectric Focusing; D007700:Kinetics; D007875:Legionella / Q000187:drug effects / Q000201:enzymology*; D008826:Microbial Sensitivity Tests; D008970:Molecular Weight; D001618:beta-Lactamases / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D001618:beta-Lactamases