Detail Information for IndEnz0018001371
IED ID IndEnz0018001371
Enzyme Type ID peroxidase001371
Protein Name Peroxiredoxin-1
EC 1.11.1.24
Thioredoxin-dependent peroxiredoxin 1
Gene Name PRDX1 GekBS014P
Organism Gekko japonicus (Schlegel's Japanese gecko)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Gekkota (geckos) Gekkonidae (geckos) Gekkoninae Gekko Gekko japonicus (Schlegel's Japanese gecko)
Enzyme Sequence MSSGNAYIGKLAPDFQATAVMPDGQFKEIKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRSEEFRKINCEVIGASVDSHFCHLAWINTPKKQGGLGSMHIPLVSDTKRVIAKDYGILKEDEGISYRGLFIIDDKGTLRQITINDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWQPGSDTIKPDVQKSKEYFSKHK
Enzyme Length 199
Uniprot Accession Number Q6DV14
Absorption
Active Site ACT_SITE 52; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:Q06830
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:0000250|UniProtKB:Q06830};
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. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). {ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (2); Domain (1)
Keywords Antioxidant;Cytoplasm;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
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. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:Q06830}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,348
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda