PMID:8270189

Citation	Goffin, C, Ayala, JA, Nguyen-Distèche, M and Ghuysen, JM (1993) Site-directed mutagenesis of dicarboxylic acid residues of the penicillin-binding module of the Escherichia coli penicillin-binding protein 3. FEMS Microbiol. Lett. 113:247-51
Abstract	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.
Links	PubMed
Keywords	Bacterial Proteins; Base Sequence; Binding Sites; Carrier Proteins; Dicarboxylic Acids/chemistry; Dicarboxylic Acids/metabolism; Enzyme Stability; Escherichia coli/enzymology; Escherichia coli Proteins; Hexosyltransferases/chemistry; Hexosyltransferases/metabolism; Hot Temperature; Molecular Sequence Data; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Mutagenesis, Site-Directed; Penicillin-Binding Proteins; Penicillins/metabolism; Peptidoglycan Glycosyltransferase; Peptidyl Transferases/chemistry; Peptidyl Transferases/metabolism; Structure-Activity Relationship
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