Hashimoto W, Suzuki H, Nohara S, Kumagai H
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Biochem Biophys Res Commun. 1992 Nov 30;189(1):173-8. doi: 10.1016/0006-291x(92)91540-7.
Arginyl residues 513 and 571 of Escherichia coli K-12 gamma-glutamyl-transpeptidase (EC 2.3.2.2) were substituted with alanyl and glycyl residues, respectively, by oligonucleotide-directed in vitro mutagenesis. Both mutants were devoid of the enzymatic activity. On Western blot analysis, we found that both mutants accumulated a gamma-glutamyltranspeptidase precursor which was not processed into large and small subunits in the periplasmic space of Escherichia coli.