Reference : The Bimodular G57-V577 Polypeptide Chain of the Class B Penicillin-Binding Protein 3 of ...
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/4054
The Bimodular G57-V577 Polypeptide Chain of the Class B Penicillin-Binding Protein 3 of Escherichia Coli Catalyzes Peptide Bond Formation from Thiolesters and Does Not Catalyze Glycan Chain Polymerization from the Lipid II Intermediate
English
Adam, Maggy [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Fraipont, Claudine mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Rhazi, Noureddine mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > > >]
Nguyen-Disteche, Martine [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > >]
Lakaye, Bernard mailto [Université de Liège - ULg > Institut de Chimie > Centre d'Ingénirie des Protéines > Laboratoire d'Enzymologie > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Institut de Chimie > Centre d'Ingénirie des Protéines > Laboratoire d'Enzymologie > >]
Devreese, Bart [Rijksunversiteit-Gent > > Laboratorium voor Eiwitbiochemie en Eiwitengineering > >]
Van Beeumen, Jozef [Rijksunversiteit-Gent > > Laboratorium voor Eiwitbiochemie en Eiwitengineering > >]
van Heijenoort, Yvelyne [Université Paris-Sud 11 > > Laboratoire de Biochimie Moléculaire et Cellulaire > >]
van Heijenoort, Jean [Université Paris-Sud 11 > > Laboratoire de Biochimie Moléculaire et Cellulaire > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > >]
Oct-1997
Journal of Bacteriology
American Society for Microbiology (ASM)
179
19
6005-6009
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] Because the specificity profile of the membrane anchor-free G57-V577 penicillin-binding protein 3 (PBP3) of Escherichia coli for a large series of beta-lactam antibiotics is similar to that of the full-size membrane-bound PBP, the truncated PBP is expected to adopt the native folded conformation. The truncated PBP3 functions as a thiolesterase. In aqueous media and in the presence of millimolar concentrations of a properly structured amino compound, it catalyzes the aminolysis of the thiolester until completion, suggesting that the penicillin-binding module of PBP3 is designed to catalyze transpeptidation reactions. In contrast, the truncated PBP3 is devoid of glycan polymerization activity on the E. coli lipid II intermediate, suggesting that the non-penicillin-binding module of PBP3 is not a transglycosylase.
Centre d'Ingénierie des Protéines - CIP
Fond de la Rercherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/4054

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