Article (Scientific journals)
A comparative study of class-D beta-lactamases.
Ledent, Philippe; Raquet, X; Joris, Bernard et al.
1993In Biochemical Journal, 292 ( Pt 2), p. 555-62
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Keywords :
Binding Sites; Catalysis; Chromatography, Affinity; Chromatography, Ion Exchange; Cloning, Molecular; Kinetics; Penicillanic Acid/metabolism; Plasmids; Serine/metabolism; Substrate Specificity; beta-Lactamases/antagonists & inhibitors/chemistry/isolation & purification/metabolism
Abstract :
[en] Three class-D beta-lactamases (OXA2, OXA1 and PSE2) were produced and purified to protein homogeneity. 6 beta-Iodopenicillanate inactivated the OXA2 enzyme without detectable turnover. Labelling of the same beta-lactamase with 6 beta-iodo[3H]penicillanate allowed the identification of Ser-70 as the active-site serine residue. In agreement with previous reports, the apparent M(r) of the OXA2 enzyme as determined by molecular-sieve filtration, was significantly higher than that deduced from the gene sequence, but this was not due to an equilibrium between a monomer and a dimer. The heterogeneity of the OXA2 beta-lactamase on ion-exchange chromatography contrasted with the similarity of the catalytic properties of the various forms. A first overview of the enzymic properties of the three 'oxacillinases' is presented. With the OXA2 enzyme, 'burst' kinetics, implying branched pathways, seemed to prevail with many substrates.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Ledent, Philippe
Raquet, X
Joris, Bernard ;  Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes
Van Beeumen, J
Frère, Jean-Marie ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Language :
English
Title :
A comparative study of class-D beta-lactamases.
Publication date :
1993
Journal title :
Biochemical Journal
ISSN :
0264-6021
eISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
292 ( Pt 2)
Pages :
555-62
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 21 May 2012

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