Soluble penicillin-binding protein 2a: beta-lactam binding and inhibition by non-beta-lactams using a 96-well format.

@article{Toney1998SolublePP,
  title={Soluble penicillin-binding protein 2a: beta-lactam binding and inhibition by non-beta-lactams using a 96-well format.},
  author={Jeffrey H. Toney and Gareth Hammond and Barbara Leiting and Kellyann D Pryor and Joseph S. K. Wu and Gregory C. Cuca and David L. Pompliano},
  journal={Analytical biochemistry},
  year={1998},
  volume={255 1},
  pages={113-9}
}
High level methicillin resistance in Staphylococcus aureus is dependent upon the acquisition of the mecA gene encoding penicillin-binding protein 2a (PBP2a). PBP2a is a member of a family of peptidoglycan biosynthetic enzymes involved in assembly of the cell wall in bacteria and is poorly inactivated by beta-lactam antibiotics. We describe a 96-well-filter binding assay using recombinant, soluble PBP2a which allows for kinetic measurement of penicillin binding. The deacylation rate constant for… CONTINUE READING