Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis.
The beta-lactamase from Bacteroides fragilis GAI-30144 hydrolyzed imipenem, oxyiminocephalosporins, cephamycins, and penicillins. Enzyme activity was inhibited by EDTA. Zinc completely reversed inactivation of the enzyme by EDTA. The molecular mass of purified enzyme was estimated to be 33,000 daltons.
Bandoh
K
K
Institute of Anaerobic Bacteriology, Gifu University School of Medicine, Japan.
Muto
Y
Y
Watanabe
K
K
Katoh
N
N
Ueno
K
K
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D001442:Bacteroides Infections / Q000276:immunology; D001441:Bacteroides fragilis / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; 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; D004492:Edetic Acid; D001618:beta-Lactamases