Article (Scientific journals)
Mono- and binuclear Zn-beta-lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions.
Paul-Soto, R.; Hernandez-Valladares, M.; Galleni, Moreno et al.
1998In FEBS Letters, 438 (1-2), p. 137-40
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Keywords :
Anti-Bacterial Agents/metabolism; Apoenzymes/metabolism; Bacteroides fragilis/enzymology; Binding Sites; Cadmium/metabolism/pharmacology; Calorimetry, Differential Scanning; Chelating Agents/pharmacology; Coenzymes/chemistry/pharmacology; Dialysis; Dithiothreitol/pharmacology; Kinetics; Picolinic Acids/pharmacology; Protein Denaturation; Spectrometry, Fluorescence; Substrate Specificity; Thermodynamics; Titrimetry; Zinc/chemistry/metabolism; beta-Lactamases/metabolism; beta-Lactams
Abstract :
[en] The Bacteroides fragilis Zn-beta-lactamase is active with a mono- and a binuclear zinc site. The apoenzyme produced by removal of both Zn ions does not recover full activity upon readdition of Zn2+ in contrast to an active mono-Zn form prepared at pH 6.0. Differences in k(cat) values observed are substrate-dependent implying distinct mechanisms for the mono- and binuclear species. The substrate profile of a Zn,Cd hybrid obtained by selective exchange of one zinc ion is different from that of the Zn2 enzyme with a remarkable 15-fold increased activity with cefoxitin as substrate.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Paul-Soto, R.
Hernandez-Valladares, M.
Galleni, Moreno ;  Université de Liège - ULiège
Bauer, R.
Zeppezauer, M.
Frère, Jean-Marie ;  Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Adolph, H. W.
Language :
English
Title :
Mono- and binuclear Zn-beta-lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions.
Publication date :
1998
Journal title :
FEBS Letters
ISSN :
0014-5793
eISSN :
1873-3468
Publisher :
Wiley-Blackwell, United States
Volume :
438
Issue :
1-2
Pages :
137-40
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
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