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; |