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Kinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine Peptidases

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  • Bêta-Lactamases
  • Enzyme Kinetics
  • Inactivators
  • Inhibitors
  • Life Sciences :: Biochemistry
  • Biophysics & Molecular Biology [F05]
  • Sciences Du Vivant :: Biochimie
  • Biophysique & Biologie Moléculaire [F05]
  • Biology


A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC and D-alanyl-D-alanine peptidases (DD-peptidases, EC is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn(2+)-containing enzymes, with very different kcat values. Inactivation of the Streptomyces sp. strain R61 extracellular DD-peptidase was not observed, and the Actinomadura sp. strain R39 DD-peptidase exhibited a low level of sensitivity to the compound.

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