| IED ID | IndEnz0018000010 |
| Enzyme Type ID | peroxidase000010 |
| Protein Name |
Glutathione peroxidase 1 GPx-1 GSHPx-1 EC 1.11.1.9 Cellular glutathione peroxidase Selenium-dependent glutathione peroxidase 1 |
| Gene Name | Gpx1 |
| Organism | Mus musculus (Mouse) |
| 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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MCAARLSAAAQSTVYAFSARPLTGGEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNSLKYVRPGGGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDPTALMTDPKYIIWSPVCRNDIAWNFEKFLVGPDGVPVRRYSRRFRTIDIEPDIETLLSQQSGNS |
| Enzyme Length | 201 |
| Uniprot Accession Number | P11352 |
| Absorption | |
| Active Site | ACT_SITE 47 |
| 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:0000305|PubMed:9195979};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000305|PubMed:9195979}; 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:0000269|PubMed:9195979};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709; Evidence={ECO:0000305|PubMed:9195979}; |
| 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 (PubMed:9195979). {ECO:0000269|PubMed:9195979}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Modified residue (12); Non-standard residue (1); Sequence caution (1); Site (1) |
| Keywords | Acetylation;Cytoplasm;Lipid metabolism;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Selenocysteine |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 7; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17242355; MOD_RES 32; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 62; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 62; /note=N6-succinyllysine; alternate; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 86; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 86; /note=N6-succinyllysine; alternate; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 112; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 112; /note=N6-succinyllysine; alternate; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 119; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 146; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 146; /note=N6-succinyllysine; alternate; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 195; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041 |
| Post Translational Modification | PTM: During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000269|PubMed:21420488}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10421798; 10428770; 10490281; 10627575; 10754271; 10759548; 10915565; 10915653; 10961904; 11043909; 11044609; 11217851; 11259653; 11311045; 11518697; 11545230; 11562367; 11579147; 11672444; 11726630; 11823528; 11893559; 11898410; 12117267; 12196344; 12368211; 12429206; 12466851; 12482825; 12492400; 12521604; 12531513; 12646716; 12654481; 12751789; 12804009; 12904583; 14610273; 14651853; 14681479; 14732290; 14871826; 15182862; 15242553; 15663476; 15698635; 15789223; 15795427; 15824117; 15827346; 15831471; 15920153; 1593944; 15983212; 16005359; 16041008; 16129095; 16177185; 16274876; 16373599; 16445905; 16463122; 16508038; 16615898; 16627788; 16636302; 16721761; 16723478; 16783635; 16831125; 16934683; 16962942; 16998864; 17047045; 17138759; 17145560; 17255533; 17420349; 17488888; 17510403; 17640558; 18299484; 18326824; 18445702; 18560803; 18602426; 18614015; 18638544; 18691391; 18727007; 18760274; 18762024; 18776938; 18799693; 19074896; 19141089; 19170177; 19352401; 19423573; 19466610; 19655411; 19801492; 19808019; 19885949; 19917877; 19944066; 19969073; 20015939; 20219985; 20306076; 20367278; 20404090; 20511341; 20578960; 20586612; 20627125; 20823099; 20828612; 20848490; 20872835; 21145306; 21193029; 21323725; 21347610; 21677750; 21782974; 21858002; 22067043; 22326323; 22343415; 22412999; 22820179; 22970191; 22974764; 23002098; 23014491; 23038251; 23287791; 23590304; 23811004; 23872112; 23874911; 23991041; 24075852; 24090658; 24194600; 24252128; 24296279; 24374371; 24597775; 24608112; 24743300; 24802396; 24952961; 24954415; 25401476; 25732191; 25811370; 26545014; 26816051; 26850477; 26930476; 27010651; 27124582; 27286733; 27363720; 27383629; 27626380; 27689697; 27796745; 27998725; 28039148; 28069738; 28070146; 28385808; 28597397; 29502249; 29908255; 30592974; 30685319; 30938680; 31059705; 32063362; 32152094; 32400101; 32784053; 32822804; 32896721; 33064252; 33222572; 34158609; 34315111; 7578676; 7667255; 8165054; 8566787; 8662233; 8720919; 8759521; 8792216; 9011320; 9126277; 9164985; 9214310; 9344593; 9370288; 9371744; 9386101; 9508085; 9603263; 9712879; 9737717; 9786216; 9788901; 9792801; 9820794; 9843785; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,329 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for H(2)O(2) (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488}; KM=29 uM for tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488}; Vmax=319 mM/min/mg enzyme toward H(2)O(2) (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488}; Vmax=182 mM/min/mg enzyme toward tert-butylperoxide (at 25 degrees Celsius, in 0.1 M phosphate buffer, pH 7.0) {ECO:0000269|PubMed:21420488}; |
| Metal Binding | |
| Rhea ID | RHEA:16833; RHEA:16834; RHEA:50708; RHEA:50709 |
| Cross Reference Brenda |