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• W1975763435 abstract "A mutant of human gamma-glutamyl transpeptidase (EC 2.3.2.2, a membrane-bound enzyme of importance in glutathione metabolism) that differs from the wild type by deletion of the putative signal peptide/anchor domain (amino acid residues 1-27) was expressed in insect cells using a baculovirus system. In contrast to the wild-type enzyme--which, as expected, was mainly cell-associated--the mutant enzyme was secreted into the medium. The mutant and wild-type enzymes were purified and found to exhibit virtually identical catalytic properties. The mutant enzyme was glycosylated and processed into two subunits, as found for the wild-type enzyme. Brefeldin A inhibited secretion of the mutant enzyme and led to its accumulation in cells. The findings indicate that gamma-glutamyl transpeptidase can be targeted to the endoplasmic reticulum in a manner that does not involve function of an amino-terminal signal/anchor domain and that this domain is involved primarily in a membrane anchoring function. Another region of the enzyme may function as a signal domain." @default.
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• W1975763435 date "1995-01-03" @default.
• W1975763435 modified "2023-09-23" @default.
• W1975763435 title "Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain." @default.
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• W1975763435 doi "https://doi.org/10.1073/pnas.92.1.126" @default.
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