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Thioredoxin reductase 3 is a selenocysteine-containing flavoenzyme that is a unique member of the thioredoxin reductase family due to its additional N-terminal glutaredoxin domain. This enables it to participate in both thioredoxin and glutathione redox systems, catalyzing disulfide bond isomerization and supporting redox homeostasis in human cells. TXNRD3 is expressed most highly in the testis, where it promotes the maturation and formation of sperm structural components via disulfide bond formation. The protein functions as a homodimer with FAD and selenocysteine at its active site, and is encoded by the TXNRD3 gene on chromosome 3. Alternative splicing and non-standard translation initiation have been observed for this gene. Disease associations include Keshan disease and pontocerebellar hypoplasia type 2D; however, its broader role in diseases related to oxidative stress is possible but incompletely defined in current results[1][3][4].
Drugs would likely act through inhibition of thioredoxin reductase activity, limiting reduction of thioredoxins and/or glutathione pathways and impairing cellular redox balance. Possible modulation of selenoprotein activity
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