Biochemical properties of beta-lactamase produced by Flavobacterium odoratum.
A constitutively produced beta-lactamase was purified from Flavobacterium odoratum GN14053. The purified enzyme gave a single protein band on polyacrylamide gel electrophoresis. The isoelectric point was 5.8, and the molecular weight was estimated to be about 26,000. The enzyme activity was inhibited by EDTA, iodine, p-chloromercuribenzoate, HgCl2, and CuSO4 but not by clavulanic acid, sulbactam, imipenem, and cephamycin derivatives. The enzyme showed a broad substrate profile, hydrolyzing oxyiminocephalosporins, cephamycins, imipenem, and some penicillins.
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004352:Drug Resistance, Microbial; D005417:Flavobacterium / Q000201:enzymology*; D008826:Microbial Sensitivity Tests; D008970:Molecular Weight; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000302:isolation & purification / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases