Peroxiredoxin 5 (PRDX5)

Peroxiredoxin 5 is a mammalian antioxidant enzyme of the peroxiredoxin family, notable for its atypical structure, high catalytic efficiency for reducing peroxides and peroxynitrite, and wide subcellular distribution (mitochondria, peroxisomes, cytosol, nucleus). It protects cells from oxidative damage and regulates apoptosis, inflammation, bone remodeling, and metabolic disease. Its expression is responsive to cellular stress and may serve as a biomarker or therapeutic target in cancer, stroke, neurodegeneration, multiple sclerosis, osteoporosis, and other diseases related to oxidative stress. PRDX5 function is modulated by thioredoxins and coenzyme A, with implications for redox regulation and cell signaling. No approved drugs currently target PRDX5 directly, but fragment screening has identified small molecules binding its active site, and altering PRDX5 can change cellular sensitivity to oxidative stress and certain chemotherapeutics.

Other names

PRDX5Prdx5Peroxiredoxin VThioredoxin-dependent peroxiredoxin 5Thioredoxin peroxidase PMP20Peroxiredoxin-5, mitochondrialTPx type VIAOEB166ACR1Alu corepressor 1Antioxidant enzyme B166

Drugs or molecules modulating PRDX5 generally act by influencing its antioxidant activity, either reducing or inhibiting peroxide detoxification, or altering cellular redox state. Thioredoxins and coenzyme A (CoA) regulate PRDX5 function through redox cycling and covalent modification.