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Glutathione S-transferase alpha 3 (GSTA3) is a human enzyme belonging to the alpha class of glutathione S-transferases, which are cytosolic enzymes involved in the detoxification of endogenous and exogenous electrophilic compounds by conjugation with reduced glutathione[1][2][8]. GSTA3 is particularly notable for its high efficiency in the double-bond isomerization of steroid intermediates, making it a key player in the biosynthesis of steroid hormones such as progesterone and testosterone[1][2][7]. This enzyme also contributes to cellular protection against toxic, carcinogenic, and pharmacologically active substances. GSTA3 is encoded by the GSTA3 gene, mapped to chromosome 6, and shares structural features with other thioredoxin fold superfamily enzymes[4][5][3][6]. Deficiencies or genetic polymorphisms in GSTA3 and related GSTs can impact cellular responses to toxins and drugs, with implications for disease susceptibility, cancer risk, and drug response.
Substrate for glutathione conjugation (as with glutathione); Modulation of bioactivation/detoxification of xenobiotics and endogenous compounds; Steroid double-bond isomerization
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