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Kinetic study of interaction between BRL 42715, beta-lactamases, and D-alanyl-D-alanine peptidases
A Matagne1, P Ledent, D Monnaie
1Laboratoire d'Enzymologie, Université de Liège, Sart-Tilman, Belgium.
Antimicrobial Agents and Chemotherapy
|January 1, 1995
Abstract:
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.