| IED ID | IndEnz0018001523 |
| Enzyme Type ID | peroxidase001523 |
| Protein Name |
Peroxiredoxin TSA2 Prx EC 1.11.1.24 Cytoplasmic thiol peroxidase 2 cTPx 2 Thiol-specific antioxidant protein 2 Thioredoxin peroxidase type Ib TPx type Ib Thioredoxin-dependent peroxiredoxin TSA2 |
| Gene Name | TSA2 YDR453C D9461.38 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MVAEVQKQAPPFKKTAVVDGIFEEISLEKYKGKYVVLAFVPLAFSFVCPTEIVAFSDAAKKFEDQGAQVLFASTDSEYSLLAWTNLPRKDGGLGPVKVPLLADKNHSLSRDYGVLIEKEGIALRGLFIIDPKGIIRHITINDLSVGRNVNEALRLVEGFQWTDKNGTVLPCNWTPGAATIKPDVKDSKEYFKNANN |
| Enzyme Length | 196 |
| Uniprot Accession Number | Q04120 |
| Absorption | |
| Active Site | ACT_SITE 48; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000305|PubMed:26894543 |
| 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:0000269|PubMed:15210711}; |
| 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 (PubMed:10681558, PubMed:11741925, PubMed:15210711). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410). {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:11741925, ECO:0000269|PubMed:15163410, ECO:0000269|PubMed:15210711}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Cross-link (3); Disulfide bond (2); Domain (1); Helix (7); Modified residue (1); Mutagenesis (1); Turn (3) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Disulfide bond;Isopeptide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Ubl conjugation |
| Interact With | |
| Induction | INDUCTION: By peroxides. {ECO:0000269|PubMed:15210711}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558}. |
| Modified Residue | MOD_RES 174; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P34760 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 5DVB; 5EPT; 6UTL; |
| Mapped Pubmed ID | 11018134; 11169096; 11283351; 11805837; 11821410; 12614847; 12824182; 15051715; 15706081; 15917183; 16554755; 17210445; 18021067; 18039473; 18084888; 18084898; 18467557; 18719252; 19106092; 19343719; 19424433; 19536198; 19538506; 19543365; 20098417; 20308573; 20846146; 21326823; 21431909; 22094416; 22209905; 22529852; 22842922; 22912562; 22970195; 23198979; 23291433; 23457300; 24022485; 24410772; 24418709; 24444374; 25173844; 25247923; 25601439; 25866393; 26261310; 26490118; 26685013; 26813659; 26837754; 26843371; 27629822; 27634403; 32615144; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,615 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.8 uM for H(2)O(2) {ECO:0000269|PubMed:15210711}; KM=4.5 uM for cumene hydroperoxide {ECO:0000269|PubMed:15210711}; KM=5.1 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:15210711}; Vmax=0.39 uM/sec/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:15210711}; Vmax=0.28 uM/sec/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:15210711}; Vmax=0.29 uM/sec/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:15210711}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |