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Title: Biochemical properties of beta-lactamase produced by Flavobacterium odoratum. Author: Sato K, Fujii T, Okamoto R, Inoue M, Mitsuhashi S. Journal: Antimicrob Agents Chemother; 1985 Apr; 27(4):612-4. PubMed ID: 3873903. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]