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

Abstract

A detailed kinetic study of the interactions between BRL 42715, a β- lactamase-inhibiting penem, and various β-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 β- lactamases but was hydrolyzed by the class B, Zn2+-containing enzymes, with very different k(cat) 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.