Open AccessBiochemical properties of beta-lactamase produced by Flavobacterium odoratum
Author(s) -
Kenichi Sato,
Tadashi Fujii,
R Okamoto,
Matsuhisa Inoue,
Susumu Mitsuhashi
Publication year - 1985
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.27.4.612
Subject(s) - isoelectric point , sulbactam , imipenem , biochemistry , enzyme , isoelectric focusing , flavobacterium , chemistry , microbiology and biotechnology , biology , antibiotics , bacteria , pseudomonas , antibiotic resistance , genetics
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.