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Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits
W Hashimoto1, H Suzuki, S Nohara
1Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Biochemical and Biophysical Research Communications
|November 30, 1992
Abstract:
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.