Glutathione-dependent enzyme

Glutathione-dependent enzymes are a broad class of proteins that utilize the tripeptide glutathione (GSH) to catalyze various biochemical reactions essential for cellular health (Hayes et al., 2005, Annual Review of Pharmacology and Toxicology). Key members include glutathione S-transferases (GSTs), which are involved in the detoxification of xenobiotics, and glutathione peroxidases (GPXs), which serve as critical antioxidants by reducing hydrogen peroxide and organic hydroperoxides (Arthur, 2000, Cellular and Molecular Life Sciences). These enzymes are vital for maintaining the cellular redox state and protecting DNA, proteins, and lipids from oxidative damage (UniProt). In clinical contexts, the overexpression of certain glutathione-dependent enzymes, particularly GSTP1, is frequently associated with resistance to chemotherapy in cancer patients, as they can conjugate and neutralize drugs (Townsend and Tew, 2003, Oncogene). Therapeutic strategies often focus on inhibiting these enzymes to enhance the efficacy of anti-cancer treatments or utilizing enzyme mimetics like Ebselen to combat oxidative stress in neurodegenerative and cardiovascular diseases (PubChem; NIH). Additionally, enzymes like leukotriene C4 synthase are involved in inflammatory signaling, making them targets for asthma and other inflammatory conditions (PubMed). Overall, this group of enzymes represents a critical interface between metabolism, defense against oxidative stress, and drug response.

Other names

Glutathione-utilizing enzymesGSH-dependent enzymesGlutathione-linked enzymes

Inhibition of glutathione S-transferase (GST) to reverse chemotherapy resistance; Catalytic reduction of hydroperoxides via glutathione peroxidase (GPX) mimicry; Depletion of intracellular glutathione (GSH) pools.