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Peroxiredoxins (Prxs) are a ubiquitous and highly conserved family of antioxidant enzymes. They play a central role in reducing peroxides, protecting cells from oxidative damage, and regulating redox signaling pathways. Prxs are thiol-dependent peroxidases that catalyze the reduction of peroxides using a conserved cysteine residue at their active site. Mammalian isoforms have distinct subcellular localizations: Cytosol/Nucleus: Peroxiredoxin 1, 2, and 6; Mitochondria: Peroxiredoxin 3; Endoplasmic Reticulum: Peroxiredoxin 4; Cytosol/Mitochondria/Peroxisomes: Peroxiredoxin 5. Prx activity can be regulated via phosphorylation and changes in redox or oligomerization states. Hyperoxidation leads to temporary enzyme inactivation until repair by sulfiredoxin occurs. Phosphorylation modulates sensitivity to extracellular signals.
Catalyzes the reduction of peroxides, including hydrogen peroxide, organic hydroperoxides, and peroxynitrite, using a conserved cysteine residue.
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