Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a.

@article{Walsh1996EnzymeKA,
  title={Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a.},
  author={Timothy R. Walsh and Stuart D. Gamblin and David C. Emery and Alasdair P Macgowan and Peter M. Bennett},
  journal={The Journal of antimicrobial chemotherapy},
  year={1996},
  volume={37 3},
  pages={423-31}
}
The metallo-beta-lactamase from Aeromonas sobria 163a, ImiS, was isolated in a two stage purification procedure using protein affinity columns. Enzyme kinetics show that ImiS hydrolyses the carbapenems but displays poor activity against other beta-lactams. ImiS possesses the narrowest spectrum of activity of the Group 3 enzymes that have been analysed. Sequencing of the 40 N-terminal amino acids show this region to be identical to that of the CphA metallo-beta-lactamase from Aeromonas… CONTINUE READING

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