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

@article{Bebrone2005DramaticBO,
  title={Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis.},
  author={Carine Bebrone and Christine Anne and Kris De Vriendt and Bart Devreese and Gian Maria Rossolini and Jozef J. Van Beeumen and J J Frere and Moreno Galleni},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 31},
  pages={28195-202}
}
Among class B beta-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… CONTINUE READING

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