Twenty β-lactam molecules, including penicillins, cephalosporins, penems, carbapenems, and monobactams, were investigated as potential substrates for Xanthomonas maltophilia ULA-511, Aeromonas hydrophila AE036, and Bacillus cereus 5/B/6 metallo-β-lactamases. A detailed analysis of the kinetic parameters examined confirmed these enzymes to be broad-spectrum β- lactamases with different ranges of catalytic efficiency. Cefoxitin and moxalactam, substrates for the β-lactamases from X. maltophilia ULA-511 and B. cereus 5/B/6, behaved as inactivators of the A. hydrophila AE036 metallo- β-lactamase, which appeared to be unique among the enzymes tested in this study. In addition, we report a new, faster, and reliable purification procedure for the B. cereus 5/B/6 metallo-β-lactamase, cloned in Escherichia coli HB101.

Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases

AMICOSANTE, Gianfranco
1995-01-01

Abstract

Twenty β-lactam molecules, including penicillins, cephalosporins, penems, carbapenems, and monobactams, were investigated as potential substrates for Xanthomonas maltophilia ULA-511, Aeromonas hydrophila AE036, and Bacillus cereus 5/B/6 metallo-β-lactamases. A detailed analysis of the kinetic parameters examined confirmed these enzymes to be broad-spectrum β- lactamases with different ranges of catalytic efficiency. Cefoxitin and moxalactam, substrates for the β-lactamases from X. maltophilia ULA-511 and B. cereus 5/B/6, behaved as inactivators of the A. hydrophila AE036 metallo- β-lactamase, which appeared to be unique among the enzymes tested in this study. In addition, we report a new, faster, and reliable purification procedure for the B. cereus 5/B/6 metallo-β-lactamase, cloned in Escherichia coli HB101.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/103160
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