Article (Scientific journals)
Site-directed mutagenesis of dicarboxylic acid residues of the penicillin-binding module of the Escherichia coli penicillin-binding protein 3
Goffin, Colette; Ayala, J. A.; Nguyen-Distèche, Martine et al.
1993In FEMS Microbiology Letters, 113 (3), p. 247-251
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Keywords :
Escherichia coli penicillin-binding protein 3; Catalytic mechanism; Site-directed mutagenesis
Abstract :
[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.
Research center :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Goffin, Colette ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Ayala, J. A.;  Universidad Autonoma - Madrid > Centro de Biologica Molecular
Nguyen-Distèche, Martine ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénieurie des Protéines
Language :
English
Title :
Site-directed mutagenesis of dicarboxylic acid residues of the penicillin-binding module of the Escherichia coli penicillin-binding protein 3
Publication date :
01 November 1993
Journal title :
FEMS Microbiology Letters
ISSN :
0378-1097
eISSN :
1574-6968
Publisher :
Blackwell Publishing, Oxford, United Kingdom
Volume :
113
Issue :
3
Pages :
247-251
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRSM - Fonds de la Recherche Scientifique Médicale [BE]
F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
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