Article (Scientific journals)
The active site of the P99 beta-lactamase from Enterobacter cloacae.
Joris, Bernard; Dusart, Jean; Frère, Jean-Marie et al.
1984In Biochemical Journal, 223 (1), p. 271-4
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Keywords :
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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Joris, Bernard ;  Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes
Dusart, Jean;  Université de Liège - ULiège > Services administratifs généraux > R&D : Gestion opérationnelle
Frère, Jean-Marie ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
van Beeumen, J
Emanuel, E L
Petursson, S
Gagnon, J
Waley, S G
Language :
English
Title :
The active site of the P99 beta-lactamase from Enterobacter cloacae.
Publication date :
1984
Journal title :
Biochemical Journal
ISSN :
0264-6021
eISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
223
Issue :
1
Pages :
271-4
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 09 June 2012

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