Open AccessSite‐directed mutagenesis of penicillin‐binding protein 3 of Escherichia coli : Role of Val‐545
Author(s) -
Ayala Juan,
Goffin Colette,
NguyenDistèche Martine,
Ghuysen JeanMarie
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07106.x
Subject(s) - escherichia coli , penicillin binding proteins , benzylpenicillin , mutagenesis , penicillin , serine , site directed mutagenesis , microbiology and biotechnology , chemistry , mechanism (biology) , binding site , biology , biochemistry , mutation , antibiotics , mutant , gene , phosphorylation , philosophy , epistemology
Val545 of the Escherichia coli penicillin‐binding protein 3 is essential to the acyl transfer mechanism through which the active‐site serine 307 is acylated by benzylpenicillin and cephalexin and to the mechanism through which the protein allows rapidly growing cells to divide.