Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4.

@article{Lassaux2011BiochemicalAS,
  title={Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4.},
  author={Patricia Lassaux and Daouda A K Traore and Elodie Loisel and Adrien Favier and Jean-Denis Docquier and Jean S{\'e}bastien Sohier and Cl{\'e}mentine Laurent and Carine Bebrone and J M Fr{\`e}re and Jean-Luc Ferrer and Moreno Galleni},
  journal={Antimicrobial agents and chemotherapy},
  year={2011},
  volume={55 3},
  pages={1248-55}
}
The metallo-β-lactamase VIM-4, mainly found in Pseudomonas aeruginosa or Acinetobacter baumannii, was produced in Escherichia coli and characterized by biochemical and X-ray techniques. A detailed kinetic study performed in the presence of Zn²+ at concentrations ranging from 0.4 to 100 μM showed that VIM-4 exhibits a kinetic profile similar to the profiles of VIM-2 and VIM-1. However, VIM-4 is more active than VIM-1 against benzylpenicillin, cephalothin, nitrocefin, and imipenem and is less… CONTINUE READING

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