Reference : Properties of a class C beta-lactamase from Serratia marcescens.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/124945
Properties of a class C beta-lactamase from Serratia marcescens.
English
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes]
De Meester, F [> > > >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques]
Masson, Séverine [Université de Liège - ULg > Département de droit > Département de droit]
Dusart, Jean [Université de Liège - ULg > Services administratifs généraux > R&D : Gestion opérationnelle]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines]
Van Beeumen, J [> > > >]
Bush, K [> > > >]
Sykes, R [> > > >]
1986
Biochemical Journal
Portland Press
239
3
581-6
Yes (verified by ORBi)
0264-6021
1470-8728
London
United Kingdom
[en] Amino Acids/analysis ; Bacterial Proteins ; Binding Sites ; Hydrogen-Ion Concentration ; Kinetics ; Osmolar Concentration ; Peptide Fragments/analysis ; Serratia marcescens/enzymology ; beta-Lactamases/isolation & purification/metabolism
[en] A beta-lactamase produced by a penicillin-resistant strain of Serratia marcescens was isolated and purified. The kcat. value for benzylpenicillin was about 5% of that observed for the best cephalosporin substrates. However, the low Km of the penam resulted in a high catalytic efficiency (kcat./Km) and the classification of the enzyme as a cephalosporinase might not be completely justified. It also exhibited a low but measurable activity against cefotaxime, cefuroxime, cefoxitin and moxalactam. Substrate-induced inactivation was observed both with a very good (cephalothin) or a very bad (moxalactam) substrate. The active site was labelled by beta-iodopenicillanate. Trypsin digestion produced a 19-residue active-site peptide whose sequence clearly allowed the classification of the enzyme as a class C beta-lactamase.
http://hdl.handle.net/2268/124945

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