ORBi: Matagne André - Kinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine Peptidases

Reference : Kinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine ...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/28927

Title :	Kinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine Peptidases
Language :	English
Author, co-author :	Matagne, André [Université de Liège - ULg > Département des sciences de la vie > Enzymologie, Centre d'Ingénierie des Protéines > >]
	Ledent, Philippe [Université de Liège - ULG > Enzymologie, Centre d'Ingénierie des Protéines > > >]
	Monnaie, Didier [Université de Liège - ULG > Enzymologie, Centre d'Ingénierie des Protéines > > >]
	Felici, Antonio [Università degli Studi dell'Aquila - UNIVAQ > > > >]
	Jamin, Marc [Université de Liège - ULG > Enzymologie, Centre d'Ingénierie des Protéines > > >]
	Raquet, X. [Université de Liège - ULG > Enzymologie, Centre d'Ingénierie des Protéines > > >]
	Galleni, Moreno [Université de Liège - ULg > Département des sciences de la vie > Enzymologie, Centre d'Ingénierie des Protéines > >]
	Klein, Daniel [ULg > Enzymologie, Centre d'Ingénierie des Protéines > > >]
	Francois, Irène [> > > >]
	Frère, Jean-Marie [Université de Liège - ULg > Département des sciences de la vie > Enzymologie, Centre d'Ingénierie des Protéines > >]
Publication date :	Jan-1995
Journal title :	Antimicrobial Agents and Chemotherapy
Volume :	39
Issue/season :	1
Pages :	227-31
Audience :	International
ISSN :	0066-4804
Keywords :	[en] bêta-lactamases ; enzyme kinetics ; inactivators ; inhibitors
Abstract :	[en] 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.
Permalink :	http://hdl.handle.net/2268/28927

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Open access	MatagnePapier BRL 42715.pdf		Publisher postprint	238.27 kB	View/Open

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