| IED ID | IndEnz0018001229 |
| Enzyme Type ID | peroxidase001229 |
| Protein Name |
Peroxiredoxin prdx-2 EC 1.11.1.24 2-Cys peroxiredoxin 2 |
| Gene Name | prdx-2 prx2 tag-56 F09E5.15 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH |
| Enzyme Length | 201 |
| Uniprot Accession Number | A0A0K3AUJ9 |
| Absorption | |
| Active Site | ACT_SITE 55; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:Q06830 |
| Activity Regulation | ACTIVITY REGULATION: Activated following oxidation of the conserved redox-active cysteine residue, which subsequently allows for the oxidation and activation of substrates. {ECO:0000269|PubMed:15099742, ECO:0000269|PubMed:19064914}. |
| 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:0000269|PubMed:15099742}; |
| 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 (PubMed:15099742). In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide (PubMed:25640076). In the intestine, plays a role in protecting cells against oxidative stress by detoxifying peroxides such as hydrogen peroxide (PubMed:15099742, PubMed:19064914, PubMed:20649472). In addition, plays a role in the recovery from oxidative stress induced by hydrogen peroxide (PubMed:20649472). In its hyperoxidized form (induced by hydrogen peroxide), confers protection against heat stress (PubMed:19064914). However, has a low tendency for overoxidation during the normal lifespan (PubMed:20964547). Increases sensitivity to cytotoxity caused by metalloids and heavy metals such as arsenic and cadmium by playing a role in inhibiting the expression of phase II detoxification genes such as gcs-1 in intestinal cells (PubMed:19064914, PubMed:25204677). In addition, in response to arsenite, promotes the secretion of the insulin ligand daf-28 into the pseudocoelom, which negatively regulates the activities of daf-16 and skn-1 (PubMed:25808059). Plays a role in promoting longevity (PubMed:19064914, PubMed:24889636). Plays a role in the mitohormetic pathway by promoting the activation of pmk-1 in response to the drug metformin (PubMed:24889636). {ECO:0000269|PubMed:15099742, ECO:0000269|PubMed:19064914, ECO:0000269|PubMed:20649472, ECO:0000269|PubMed:20964547, ECO:0000269|PubMed:24889636, ECO:0000269|PubMed:25204677, ECO:0000269|PubMed:25640076, ECO:0000269|PubMed:25808059}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (2); Domain (1) |
| Keywords | Alternative splicing;Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to the drug metformin. {ECO:0000269|PubMed:24889636}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19064914}. |
| Modified Residue | |
| 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. {ECO:0000250|UniProtKB:Q06830}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11231151; 15338614; 16673436; 17850180; 19922876; 21085631; 21177967; 21367940; 22560298; 23800452; 25487147; 26255886; 26759963; 26904949; 27506200; 31216475; 34488090; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,413 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |