| IED ID | IndEnz0018000172 |
| Enzyme Type ID | peroxidase000172 |
| Protein Name |
Glutathione peroxidase 1 GPx-1 GSHPx-1 EC 1.11.1.9 Cellular glutathione peroxidase |
| Gene Name | GPX1 |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MCAAQRSAAALAAVAPRSVYAFSARPLAGGEPISLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNGEILNCLKYVRPGGGFEPNFMLFEKCEVNGANAHPLFAFLREALPTPSDDATALMTDPKFITWSPVCRNDIAWNFEKFLVGPDGVPLRRYSRRFLTIDIEPDIEALLSQEPSSA |
| Enzyme Length | 206 |
| Uniprot Accession Number | Q8MJ14 |
| Absorption | |
| Active Site | ACT_SITE 52; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000250|UniProtKB:P11352};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000250|UniProtKB:P11352}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90680; Evidence={ECO:0000250|UniProtKB:P11352};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709; Evidence={ECO:0000250|UniProtKB:P11352}; |
| DNA Binding | |
| EC Number | 1.11.1.9 |
| Enzyme Function | FUNCTION: Protects the hemoglobin in erythrocytes from oxidative breakdown. In platelets, plays a crucial role of glutathione peroxidase in the arachidonic acid metabolism. {ECO:0000250|UniProtKB:P11352}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Modified residue (9); Non-standard residue (1); Site (1) |
| Keywords | Acetylation;Cytoplasm;Lipid metabolism;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Selenocysteine |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 37; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 91; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 91; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 117; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 117; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 151; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 151; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 200; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 204; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P07203 |
| Post Translational Modification | PTM: During periods of oxidative stress, Sec-52 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16908641; 22580339; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,591 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16833; RHEA:16834; RHEA:50708; RHEA:50709 |
| Cross Reference Brenda |