Glutathione S-transferase omega-2 (GSTO2)

Glutathione S-transferase omega-2 is an omega-class cytosolic enzyme of the glutathione S-transferase superfamily, uniquely characterized by a cysteine-containing active site (as opposed to the serine or tyrosine in other GST classes) that enables distinct redox functions[1][2][3]. It catalyzes glutathione-dependent reduction reactions, including the reduction of dehydroascorbate and monomethylarsonic acid, contributing to cellular antioxidant defenses and the detoxification of endogenous and xenobiotic compounds. In mammals, GSTO2 plays a unique role in fertilization by facilitating sperm nuclear decondensation upon entry into the oocyte[1]. Disease-related polymorphisms in GSTO2 have been associated with various cancers, neurodegenerative conditions, and age-related diseases[2][4]. It remains a target of pharmacological interest for antioxidant modulation and chemoprotection, but specific inhibitory drugs for GSTO2 are primarily in the experimental phase[2].

Other names

Glutathione S-transferase omega-2GSTO2GSTO-2MMA(V) reductaseglutathione-dependent dehydroascorbate reductasemonomethylarsonic acid reductasebA127L20.1

Active site inhibition (irreversible binding to the cysteine in the enzyme’s catalytic domain, preventing glutathione conjugation and reduction reactions); Redox modulation (alteration of cellular redox state by disrupting glutathione-mediated detoxification pathways); Blocking downstream detoxification and antioxidant defense may potentiate therapeutic or toxic effects depending on context.