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Characterization of a beta‐lactamase from Mycobacterium smegmatis SN2
Author(s) -
Basu Dhiman,
Narayankumar D. V.,
Van Beeumen Josef,
Basu Joyoti
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700204361
Subject(s) - mycobacterium smegmatis , aztreonam , microbiology and biotechnology , chemistry , enzyme , sulbactam , beta lactamase inhibitors , beta lactamase , beta (programming language) , biochemistry , mycobacterium tuberculosis , biology , antibiotic resistance , antibiotics , medicine , tuberculosis , escherichia coli , gene , imipenem , pathology , computer science , programming language
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.