Among class B β3-lactamases, the subclass B2 CphA enzyme is characterized by a unique specificity profile. CphA efficiently hydrolyzes only carbapenems. In this work, we generated site-directed mutants that possess a strongly broadened activity spectrum when compared with the WT CphA. Strikingly, the N116H/N220G double mutant exhibits a substrate profile close to that observed for the broad spectrum subclass B1 enzymes. The double mutant is significantly activated by the binding of a second zinc ion under conditions where the WT enzyme is non-competitively inhibited by the same ion. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

Bebrone, C., Anne, C., DE VRIENDT, K., Devreese, B., Rossolini, G.M., VAN BEEUMEN, J., et al. (2005). Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 280(31), 28195-28202 [10.1074/jbc.M414052200].

Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis

ROSSOLINI G. M.;
2005-01-01

Abstract

Among class B β3-lactamases, the subclass B2 CphA enzyme is characterized by a unique specificity profile. CphA efficiently hydrolyzes only carbapenems. In this work, we generated site-directed mutants that possess a strongly broadened activity spectrum when compared with the WT CphA. Strikingly, the N116H/N220G double mutant exhibits a substrate profile close to that observed for the broad spectrum subclass B1 enzymes. The double mutant is significantly activated by the binding of a second zinc ion under conditions where the WT enzyme is non-competitively inhibited by the same ion. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
2005
Bebrone, C., Anne, C., DE VRIENDT, K., Devreese, B., Rossolini, G.M., VAN BEEUMEN, J., et al. (2005). Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 280(31), 28195-28202 [10.1074/jbc.M414052200].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/8347
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