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]
Ghuysen, Serine β-lactamases and penicillin-binding proteins (1991) Annu. Rev. Microbiol., 45, pp. 37-67
Lamotte-Brasseur, Dive, Dideberg, Charlier, Frère, Ghuysen, Mechanism of acyl transfer by class A serine β-lactamase of Streptomyces albus (1991) G. Biochem. J., 279, pp. 213-221
Strynadka, Adachi, Jensen, Johns, Sielecki, Betzel, Sutoh, James, Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution (1992) Nature, 359, pp. 700-705
Bowler, Spratt, Membrane topology of penicillin-binding protein 3 of Escherichia coli (1989) Mol. Microbiol., 3, pp. 1277-1286
Englebert, Piras, El Kharroubi, Joris, Coyette, Ngnyen-Distèche, Ghuysen, Modular design of the bi(multi?)functional penicillin-binding proteins (1992) Bacterial Growth and Lysis. Metabolism and Structure of the Bacterial Sacculus, pp. 919-933. , M.A. de Pedro, J.V. Höltj, W. Löffelhardt, 2nd Edition, FEMS Symposium Proceedings. Lluc, Mallorca, Spain, Plenum Publishing Co. Ltd
Adachi, Ishiguro, Imajoh, Ohta, Mutsuzawa, Active-site residues of the transpeptidase domain of penicillin-binding protein 2 from Escherichia coli: similarity in catlytic mechanism to class A β-lactamases (1992) Biochemistry, 31, pp. 430-437
Sambrook, Fritsch, Maniatis, (1989) Molecular Cloning: A Laboratory Manual, , 2nd Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
Vieira, Messing, The pUC plasmids on M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers (1982) Gene, 19, pp. 259-268
Gibson, Studies on the Epstein-Barr virus genome (1984) Ph. D. Thesis, , 2nd Edition, Cambridge University, UK
Garcia del Portillo, de Pedro, Ayala, Identification of a new mutation in E. coli that suppresses a pbpB(Ts) phenotype in the presence of PBP1B (1991) FEMS Microbiol. Lett., 84, pp. 7-14
Kramer, Kramer, Fritz, Different base/base mismatches are corrected with different efficiencies by methyl-directed DNA mismatch-repair system of E. coli (1984) Cell, 38, pp. 879-887
Broome-Smith, Spratt, Deletion of the penicillin-binding protein 6 gene of E. coli (1982) J. Bacteriol., 152, pp. 904-906
Hedge, Spratt, Amino acid substitutions that reduce the affinity of penicillin-binding protein 3 of Escherichia coli for cephalexin (1985) Eur. J. Biochem., 151, pp. 111-121
Oefner, D'Arcy, Daley, Gubernator, Charnas, Heinze, Hubschwerlen, Winkler, Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism of β-lactam hydrolysis (1990) Nature, 343, pp. 284-288