| IED ID | IndEnz0018001385 |
| Enzyme Type ID | peroxidase001385 |
| Protein Name |
Peroxiredoxin-2 EC 1.11.1.24 Thiol-specific antioxidant protein TSA Thioredoxin peroxidase 1 Thioredoxin-dependent peroxide reductase 1 Thioredoxin-dependent peroxiredoxin 2 Fragment |
| Gene Name | PRDX2 TDPX1 |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | LFFYPLDFTFVCPTEIIAFSDRAEEFHQLGCEVLGVSVDXQXTHLAWINTPRKEGGLGPLKIPLLADVTRNLSLDYGVLKEDEGIAYRGLFIIDGKGVLRQITVNDLPVGRXVDEALRLVQGXQYTD |
| Enzyme Length | 127 |
| Uniprot Accession Number | P52552 |
| Absorption | |
| Active Site | ACT_SITE 12; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P32119 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:P32119}; |
| DNA Binding | |
| EC Number | 1.11.1.24 |
| Enzyme Function | 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). {ECO:0000250|UniProtKB:P32119}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Domain (1); Modified residue (1); Non-terminal residue (2) |
| Keywords | Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}. |
| Modified Residue | MOD_RES 73; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P32119 |
| Post Translational Modification | PTM: 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. {ECO:0000250|UniProtKB:P32119, ECO:0000250|UniProtKB:Q06830}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 14,168 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |