Characterization of a beta-lactamase from Mycobacterium smegmatis SN2.
Beta-lactamases have been reported to be largely responsible for beta-lactam resistance in Mycobacteria. We report the characterization of a cell-associated beta-lactamase from Mycobacterium smegmatis. The enzyme hydrolyzed the "beta-lactamase-stable" oximinocephalosporins. Nitrocefin was the best substrate. 6-Beta-iodopenicillanate, clavulanate and sulbactam were effective inhibitors, whereas the Ki value for aztreonam was high. From its substrate and inhibitor profile, the enzyme appeared to be a cephalosporinase of group 2e.
Basu
D
D
Department of Chemistry, Bose Institute, Calcutta, India.
Narayankumar
D V
DV
Van Beeumen
J
J
Basu
J
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D019818:Clavulanic Acid / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D008969:Molecular Sequence Data; D009161:Mycobacterium / Q000201:enzymology*; D010397:Penicillanic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D016415:Sequence Alignment; D013379:Substrate Specificity; D013407:Sulbactam / Q000494:pharmacology; D018440:beta-Lactam Resistance; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D065093:beta-Lactamase Inhibitors; D019818:Clavulanic Acid; D010397:Penicillanic Acid; C031528:6-iodopenicillanic acid; D001618:beta-Lactamases; D013407:Sulbactam