A. Matagne et al., KINETIC-STUDY OF INTERACTION BETWEEN BRL-42715, BETA-LACTAMASES, AND D-ALANYL-D-ALANINE PEPTIDASES, Antimicrobial agents and chemotherapy, 39(1), 1995, pp. 227-231
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 3.4.1.16.4) is pr
esented. The compound was a very efficient inactivator of all active-s
ite serine beta-lactamases but was hydrolyzed by the class B, Zn2+-con
taining enzymes, with very different k(cat) values. Inactivation of th
e Streptomyces sp. strain R61 extracellular DD peptidase was not obser
ved, and the Actinomadura sp. strain R39 DD-peptidase exhibited a low
level of sensitivity to the compound.