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. 1995 Jan;39(1):227–231. doi: 10.1128/aac.39.1.227

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

A Matagne 1, P Ledent 1, D Monnaie 1, A Felici 1, M Jamin 1, X Raquet 1, M Galleni 1, D Klein 1, I François 1, J M Frère 1
PMCID: PMC162513  PMID: 7695311

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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