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    Biochem Biophys Res Commun. 1992 Nov 30;189(1):173-8.

    Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits.

    Hashimoto W, Suzuki H, Nohara S, Kumagai H.

    Source

    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.

    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.

    PMID:
    1360205
    [PubMed - indexed for MEDLINE]

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