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Glutathione synthesis pathway enzymes comprise a set of key enzymes—primarily glutamate–cysteine ligase (catalyzes the rate-limiting step: synthesis of γ-glutamylcysteine from glutamate and cysteine) and glutathione synthetase (adds glycine to γ-glutamylcysteine to form glutathione)—responsible for de novo glutathione biosynthesis in nearly all mammalian cells. Glutathione maintains cellular redox balance, detoxifies xenobiotics, supports immune function, and regulates apoptosis, among other roles. Dysregulation of its synthesis is associated with cancer chemoresistance, liver disease, neurodegeneration, and other disorders. Because the term "glutathione synthesis pathway enzymes" refers to a biochemical pathway rather than a single protein, it is not a precise molecular drug target; each component should be referenced individually for structured data and drug development purposes.
Inhibitors decrease glutathione synthesis, sensitizing cells to oxidative stress; Indirect enhancement or depletion of intracellular GSH pools; In the context of cancer, lowering GSH can overcome chemoresistance.
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