| IED ID | IndEnz0018000060 |
| Enzyme Type ID | peroxidase000060 |
| Protein Name |
Peroxiredoxin AHP1 Prx EC 1.11.1.24 Alkyl hydroperoxide reductase AHPC1 Cytoplasmic thiol peroxidase 3 cTPx 3 Thiol-specific antioxidant II TSA II Thioredoxin peroxidase type II TPx type II Thioredoxin-dependent peroxiredoxin AHP1 |
| Gene Name | AHP1 YLR109W L2916 L9354.5 |
| 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 | MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL |
| Enzyme Length | 176 |
| Uniprot Accession Number | P38013 |
| Absorption | |
| Active Site | ACT_SITE 62; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000305|PubMed:22474296 |
| 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:10391912, 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. Preferentially eliminates organic peroxides rather than hydrogen peroxide (PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation (PubMed:20145245). Involved in cellular Mn(2+) homeostasis (PubMed:10635552). {ECO:0000269|PubMed:10391912, ECO:0000269|PubMed:10635552, ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:20145245, ECO:0000269|PubMed:9988687}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:9888818}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Cross-link (3); Disulfide bond (3); Domain (1); Helix (8); Initiator methionine (1); Modified residue (4); Mutagenesis (4); Sequence conflict (3); Turn (2) |
| Keywords | 3D-structure;Acetylation;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Isopeptide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Ubl conjugation |
| Interact With | P34230 |
| Induction | INDUCTION: By H(2)O(2). {ECO:0000269|PubMed:10681558}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000269|Ref.4; MOD_RES 28; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 59; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956; MOD_RES 116; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198 |
| Post Translational Modification | PTM: Conjugated to URM1, a ubiquitin-like protein. {ECO:0000269|PubMed:14555475, ECO:0000269|PubMed:21209336}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 4DSQ; 4DSR; 4DSS; 4H86; 4OWY; 7BVV; |
| Mapped Pubmed ID | 11018134; 11078740; 11169096; 11401713; 11719517; 11805837; 12270680; 12668662; 14616057; 14660704; 14739647; 15051715; 16272220; 16554755; 17576017; 18021067; 18039473; 18084888; 18201562; 19047990; 19424433; 19536198; 19538506; 19543365; 19930686; 20370606; 20508643; 20846146; 20959147; 21431909; 21444828; 21549177; 21695049; 21933953; 22094416; 22209905; 22932216; 22952687; 22970195; 23198979; 23870129; 24418709; 24444374; 25173100; 25173844; 25247923; 25898401; 25995378; 26261310; 26685013; 26813659; 26824473; 27143390; 27536287; 27937809; 32004955; 32531362; |
| Motif | |
| Gene Encoded By | |
| Mass | 19,115 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for H(2)O(2) {ECO:0000269|PubMed:9888818}; KM=14 uM for H(2)O(2) {ECO:0000269|PubMed:10391912}; KM=8 uM for cumene hydroperoxide {ECO:0000269|PubMed:9888818}; KM=45 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:9888818}; KM=76.9 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:22474296}; KM=3 uM for TRX1 {ECO:0000269|PubMed:9888818}; KM=2 uM for TRX2 {ECO:0000269|PubMed:9888818}; KM=1.3 uM for TRX2 {ECO:0000269|PubMed:22474296}; Vmax=20 umol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:9888818}; Vmax=14 umol/min/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:9888818}; Vmax=17 umol/min/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:9888818}; Vmax=17 umol/min/mg enzyme for TRX1 {ECO:0000269|PubMed:9888818}; Vmax=16 umol/min/mg enzyme for TRX2 {ECO:0000269|PubMed:9888818}; |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |