| Post Translational Modifications | The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. Acetylation increases resistance to transition to high molecular-mass complexes. Deacetylated by HDAC6 which decreases reducing activity. |
| Function | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). |
| Protein Name | Peroxiredoxin-2Natural Killer Cell-Enhancing Factor BNkef-BPrpThiol-Specific Antioxidant ProteinTsaThioredoxin Peroxidase 1Thioredoxin-Dependent Peroxide Reductase 1Thioredoxin-Dependent Peroxiredoxin 2 |
| Database Links | Reactome: R-HSA-3299685Reactome: R-HSA-5628897Reactome: R-HSA-8862803 |
| Cellular Localisation | Cytoplasm |
| Alternative Protein Names | Peroxiredoxin-2 proteinNatural Killer Cell-Enhancing Factor B proteinNkef-B proteinPrp proteinThiol-Specific Antioxidant Protein proteinTsa proteinThioredoxin Peroxidase 1 proteinThioredoxin-Dependent Peroxide Reductase 1 proteinThioredoxin-Dependent Peroxiredoxin 2 proteinPRDX2 proteinNKEFB proteinTDPX1 protein |
Information sourced from Uniprot.org
