| IED ID | IndEnz0018001690 |
| Enzyme Type ID | peroxidase001690 |
| Protein Name |
Peroxiredoxin TSA1 Prx EC 1.11.1.24 Cytoplasmic thiol peroxidase 1 cTPx 1 Protector protein PRP Thiol-specific antioxidant protein 1 Thioredoxin peroxidase type Ia TPx type Ia Thioredoxin-dependent peroxide reductase Thioredoxin-dependent peroxiredoxin TSA1 |
| Gene Name | TSA1 TPX1 TSA ZRG14 YML028W |
| 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 | MVAQVQKQAPTFKKTAVVDGVFDEVSLDKYKGKYVVLAFIPLAFTFVCPTEIIAFSEAAKKFEEQGAQVLFASTDSEYSLLAWTNIPRKEGGLGPINIPLLADTNHSLSRDYGVLIEEEGVALRGLFIIDPKGVIRHITINDLPVGRNVDEALRLVEAFQWTDKNGTVLPCNWTPGAATIKPTVEDSKEYFEAANK |
| Enzyme Length | 196 |
| Uniprot Accession Number | P34760 |
| Absorption | |
| Active Site | ACT_SITE 48; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000305|PubMed:8041739 |
| Activity Regulation | |
| Binding Site | BINDING 124; /note="Substrate"; /evidence="ECO:0000269|PubMed:22985967, ECO:0007744|PDB:3SBC" |
| 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:9888818}; |
| 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:2895105, PubMed:7961686, PubMed:10681558, PubMed:15210711, PubMed:19106090). Protects the cell against the oxidative stress caused by nascent-protein misfolding and aggregation (PubMed:24424024). Relays hydrogen peroxide as a signal to the transcription factor YAP1 by inducing the formation of intramolecular disulfide bonds in YAP1, which causes its nuclear accumulation and activation (PubMed:15706081, PubMed:19106090). 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:15163410, ECO:0000269|PubMed:15210711, ECO:0000269|PubMed:15706081, ECO:0000269|PubMed:19106090, ECO:0000269|PubMed:24424024, ECO:0000269|PubMed:2895105, ECO:0000269|PubMed:7961686}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (7); Binding site (1); Chain (1); Cross-link (3); Disulfide bond (3); Domain (1); Helix (7); Initiator methionine (1); Modified residue (1); Mutagenesis (2); Region (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Isopeptide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:18271751, ECO:0000269|PubMed:24424024, ECO:0000269|PubMed:8344960}. Note=Associates with ribosomes (PubMed:18271751). Colocalizes with sites of protein aggregation adjacent to active mitochondria (PubMed:24424024). {ECO:0000269|PubMed:18271751, ECO:0000269|PubMed:24424024}. |
| Modified Residue | MOD_RES 174; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" |
| 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 SRX1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000269|PubMed:14586471}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3SBC; |
| Mapped Pubmed ID | 10347154; 10688190; 10930459; 10978274; 11013218; 11018134; 11078740; 11169096; 11283351; 11679167; 11741925; 11749968; 11805826; 12972632; 14616057; 14690591; 15051715; 15184655; 15386117; 15917183; 16251355; 16272220; 16284124; 16361226; 16429126; 16441666; 16463173; 16507144; 16554755; 16862604; 17043098; 17121842; 17210445; 17360454; 17559233; 17651441; 17689491; 18021067; 18039473; 18084888; 18084898; 18281480; 18496816; 18552404; 18591251; 18719252; 18725414; 19106092; 19343713; 19343719; 19363031; 19424433; 19538506; 19543365; 19756144; 19851444; 20139087; 20145245; 20308573; 20463880; 20496120; 20508643; 20538604; 20729566; 20858222; 20934449; 20958246; 20959147; 21115478; 21179020; 21431909; 21549177; 21713403; 21734642; 21789324; 21884982; 21912624; 21933953; 22094416; 22209905; 22311637; 22403727; 22529852; 22685415; 22770215; 22842922; 22970195; 23198979; 23217712; 23291433; 23414292; 23457300; 23590194; 23605494; 23837470; 24022485; 24336748; 24374640; 24376879; 24410772; 24418709; 24449905; 25083872; 25173844; 25247923; 25344683; 25600293; 25601439; 25620600; 25866393; 26261310; 26335398; 26338708; 26490118; 26545110; 26685013; 2668950; 26813659; 27193513; 27264606; 27312010; 27432887; 27629822; 27634403; 27693354; 30701970; 31580947; 32662770; 7832460; 7916964; 8663080; 9799566; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,590 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for H(2)O(2) {ECO:0000269|PubMed:9888818}; KM=4 uM for cumene hydroperoxide {ECO:0000269|PubMed:9888818}; KM=10 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:9888818}; KM=2 uM for TRX1 {ECO:0000269|PubMed:9888818}; KM=3 uM for TRX2 {ECO:0000269|PubMed:9888818}; KM=12 uM for H(2)O(2) {ECO:0000269|PubMed:15210711}; KM=17.1 uM for cumene hydroperoxide {ECO:0000269|PubMed:15210711}; KM=7.9 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:15210711}; Vmax=4.8 umol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:9888818}; Vmax=2.2 umol/min/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:9888818}; Vmax=2.4 umol/min/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:9888818}; Vmax=5.5 umol/min/mg enzyme for TRX1 {ECO:0000269|PubMed:9888818}; Vmax=5.5 umol/min/mg enzyme for TRX2 {ECO:0000269|PubMed:9888818}; Vmax=0.66 uM/sec/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:15210711}; Vmax=0.56 uM/sec/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:15210711}; Vmax=0.61 uM/sec/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:15210711}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |