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Multi‐faceted regulation of γ‐glutamylcysteine synthetase
Author(s) -
Soltaninassab Syrus R.,
Sekhar Konjeti R.,
Meredith Michael J.,
Freeman Michael L.
Publication year - 2000
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/(sici)1097-4652(200002)182:2<163::aid-jcp4>3.0.co;2-1
Subject(s) - glutathione synthetase , biochemistry , glutathione , enzyme , protein subunit , transcription (linguistics) , microbiology and biotechnology , metalloprotein , transcriptional regulation , cysteine , chemistry , biology , transcription factor , gene , linguistics , philosophy
Glutathione is an important antioxidant that is involved in numerous cellular activities. γ‐Glutamylcysteine synthetase (γGCS) is a key regulatory enzyme in the synthesis of glutathione. It is a heterodimeric zinc metalloprotein that belongs to a unique class of proteins that gain activity due to formation of a reversible disulfide bond. The two subunits of γGCS exhibit differential and coordinate transcription regulation. In addition, the subunits are regulated at the posttranscriptional and posttranslational levels. These various levels of regulation allow numerous stimuli to induce or inhibit activity. J. Cell. Physiol. 182:163–170, 2000. © 2000 Wiley‐Liss, Inc.