ORBi: Joris Bernard - The active site of the P99 beta-lactamase from Enterobacter cloacae.

Reference : The active site of the P99 beta-lactamase from Enterobacter cloacae.


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/124791

Title :	The active site of the P99 beta-lactamase from Enterobacter cloacae.
Language :	English
Author, co-author :	Joris, Bernard [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes]
	Dusart, Jean [Université de Liège - ULg > Services administratifs généraux > R&D : Gestion opérationnelle]
	Frère, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines]
	van Beeumen, J [> > > >]
	Emanuel, E L [> > > >]
	Petursson, S [> > > >]
	Gagnon, J [> > > >]
	Waley, S G [> > > >]
Publication date :	1984
Journal title :	Biochemical Journal
Publisher :	Portland Press
Volume :	223
Issue/season :	1
Pages :	271-4
ISSN :	0264-6021
e-ISSN :	1470-8728
City :	London
Country :	United Kingdom
Keywords :	[en] Amino Acids/analysis ; Binding Sites ; Chromatography, High Pressure Liquid ; Enterobacter/enzymology ; Enterobacteriaceae/enzymology ; Peptide Fragments/analysis ; beta-Lactamases
Abstract :	[en] Labelling the beta-lactamase of Enterobacter cloacae P99 with a poor substrate or a mechanism-based inactivator points to an active-site serine residue in a sequence closely resembling that of the ampC beta-lactamase. These results establish the P99 enzyme as a class-C beta-lactamase, and the concurrence of the two approaches helps to confirm the reliability of determining active-site sequences with the aid of mechanism-based inactivators.
Permalink :	http://hdl.handle.net/2268/124791

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