IED ID | IndEnz0018001450 |
Enzyme Type ID | peroxidase001450 |
Protein Name |
1-Cys peroxiredoxin EC 1.11.1.- 1-CysPxn Thioredoxin peroxidase |
Gene Name | |
Organism | Dirofilaria immitis (Canine heartworm) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Spirurina Spiruromorpha Filarioidea Onchocercidae Dirofilaria Dirofilaria immitis (Canine heartworm) |
Enzyme Sequence | MTKGILLGDKFPDFRAETNEGFIPSFYDWIGKDSWAILFSHPRDFTPVCTTELARLVQLAPEFKKRNVKLIGLSCDSAESHRKWVDDIMAVCKMKCNDGDTCCSGNKLPFPIIADENRFLATELGMMDPDERDENGNALTARCVFIIGPEKTLKLSILYPATTGRNFDEILRVVDSLQLTAVKLVATPVDWKGGDDCVVLPTIDDTEAKKLFGEKINTIELPSGKHYLRMVAHPK |
Enzyme Length | 235 |
Uniprot Accession Number | O17433 |
Absorption | |
Active Site | ACT_SITE 49; /evidence=ECO:0000250; ACT_SITE 49; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P30041 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; Evidence={ECO:0000269|PubMed:10726990}; |
DNA Binding | |
EC Number | 1.11.1.- |
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. {ECO:0000269|PubMed:10726990}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Sequence conflict (2) |
Keywords | Antioxidant;Cytoplasm;Oxidoreductase;Peroxidase;Redox-active center |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 26,298 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.28 mM for H(2)O(2) {ECO:0000269|PubMed:10726990}; Vmax=16 umol/min/mg enzyme {ECO:0000269|PubMed:10726990}; |
Metal Binding | |
Rhea ID | RHEA:10008 |
Cross Reference Brenda |