Kinetic study of interaction between BRL 42715, beta-lactamases, and D-alanyl-D-alanine peptidases.

نویسندگان

  • A Matagne
  • P Ledent
  • D Monnaie
  • A Felici
  • M Jamin
  • X Raquet
  • M Galleni
  • D Klein
  • I François
  • J M Frère
چکیده

A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4) 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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عنوان ژورنال:
  • Antimicrobial agents and chemotherapy

دوره 39 1  شماره 

صفحات  -

تاریخ انتشار 1995