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.
|Titolo:||Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases|
|Autori interni:||AMICOSANTE, Gianfranco|
|Data di pubblicazione:||1995|
|Rivista:||ANTIMICROBIAL AGENTS AND CHEMOTHERAPY|
|Appare nelle tipologie:||1.1 Articolo in rivista|