Reference : Site-directed mutagenesis of dicarboxylic acid residues of the penicillin-binding module...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/86760
Site-directed mutagenesis of dicarboxylic acid residues of the penicillin-binding module of the Escherichia coli penicillin-binding protein 3
English
Goffin, Colette mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > >]
Ayala, J. A. [Universidad Autonoma - Madrid > Centro de Biologica Molecular > > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Centre d'ingénieurie des Protéines > > >]
1-Nov-1993
FEMS Microbiology Letters
Blackwell Publishing
113
3
247-251
Yes (verified by ORBi)
International
0378-1097
1574-6968
Oxford
United Kingdom
[en] Escherichia coli penicillin-binding protein 3 ; Catalytic mechanism ; Site-directed mutagenesis
[en] The glutamic acid E396, aspartic acid D409 and glutamic acid E411 residues of the Escherichia coli penicillin-binding protein 3 were each converted into an alanine residue. As deduced from penicillin-binding and complementation experiments, none of these dicarboxylic acid residues is involved in the mechanism of acylation by penicillin and none of them is essential for the in vivo functioning of the PBP. The mutation E396, however, causes an increased thermolability of the protein.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique Médicale - FRSM ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals
http://hdl.handle.net/2268/86760
10.1111/j.1574-6968.1993.tb06522.x

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