KINETIC-STUDY OF INTERACTION BETWEEN BRL-42715, BETA-LACTAMASES, AND D-ALANYL-D-ALANINE PEPTIDASES

Citation
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
Citations number
25
Categorie Soggetti
Pharmacology & Pharmacy",Microbiology
ISSN journal
00664804
Volume
39
Issue
1
Year of publication
1995
Pages
227 - 231
Database
ISI
SICI code
0066-4804(1995)39:1<227:KOIBBB>2.0.ZU;2-3
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 3.4.1.16.4) 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.