Crystal structure of BRL 42715, C6-(N1-Methyl-1,2,3-triazolylmethylene) penem, in complex with Enterobacter cloacae 908R β-lactamase: Evidence for a stereoselective mechanism from docking studies

Catherine Michaux, Paulette Charlier, Jean Marie Frère, Johan Wouters

Research output: Contribution to journalArticle

Abstract

BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial β-lactamases. The crystal structure of Enterobacter cloacae 908R class C β-lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C β-lactamase.

Original languageEnglish
Pages (from-to)3262-3263
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number10
DOIs
Publication statusPublished - 16 Mar 2005

Fingerprint Dive into the research topics of 'Crystal structure of BRL 42715, C6-(N1-Methyl-1,2,3-triazolylmethylene) penem, in complex with Enterobacter cloacae 908R β-lactamase: Evidence for a stereoselective mechanism from docking studies'. Together they form a unique fingerprint.

  • Cite this