| IED ID | IndEnz0018000017 |
| Enzyme Type ID | peroxidase000017 |
| Protein Name |
Glutathione peroxidase 1 GPx-1 GSHPx-1 EC 1.11.1.9 Cellular glutathione peroxidase |
| Gene Name | GPX1 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA |
| Enzyme Length | 203 |
| Uniprot Accession Number | P07203 |
| Absorption | |
| Active Site | ACT_SITE 49 |
| 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:11115402};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000305|PubMed:11115402}; 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:11115402};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709; Evidence={ECO:0000305|PubMed:11115402}; |
| 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:11115402). {ECO:0000269|PubMed:11115402}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Beta strand (7); Chain (1); Helix (10); Modified residue (9); Natural variant (5); Non-standard residue (1); Sequence conflict (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Lipid metabolism;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Selenocysteine |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 34; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 88; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 88; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 114; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 114; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 148; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 148; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 197; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 201; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:24275569 |
| Post Translational Modification | PTM: During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2F8A; |
| Mapped Pubmed ID | 10549853; 10833429; 10919671; 11103801; 11112379; 11823528; 12221075; 12447480; 12531513; 12655278; 12732844; 12751788; 12787913; 12810669; 12829378; 12832449; 12893824; 12893830; 14671197; 14744747; 14962293; 14962975; 15125229; 15149466; 15167446; 15192016; 15203190; 15298967; 15318035; 15774926; 15829318; 15878749; 15946795; 15990458; 16132718; 16230136; 16287877; 16354666; 16413612; 16424062; 16523188; 16538174; 16543247; 16614101; 16615267; 16627788; 16797832; 16868544; 16945136; 16956821; 16979635; 17052796; 17097614; 17149600; 17171548; 17275003; 17334644; 17526193; 17548672; 17601350; 17625244; 17634480; 17693525; 17825092; 17850515; 18186040; 18267129; 18298806; 18417962; 18449862; 18469277; 18483336; 18541150; 18541588; 18563616; 18600213; 18676680; 18806750; 18853169; 18940188; 18977241; 19012493; 19026164; 19035188; 19056482; 19124506; 19125369; 19161995; 19170196; 19195504; 19195803; 19228881; 19254950; 19285650; 19347979; 19415410; 19423521; 19424819; 19428376; 19428448; 19488773; 19505917; 19527700; 19560448; 19573080; 19578796; 19692168; 19705749; 19733578; 19773279; 19819955; 19826042; 19896490; 19913121; 19929244; 19944066; 19946932; 19949914; 19951064; 20041472; 20070187; 20082261; 20097730; 20109103; 20178852; 20200426; 20219985; 20301895; 20303587; 20306294; 20307617; 20378690; 20441054; 20444272; 20471990; 20480816; 20530237; 20578157; 20628086; 20643115; 20644561; 20724907; 20727719; 20802378; 20813000; 20851292; 20852007; 20877264; 20877624; 20878976; 21045266; 21048031; 21052528; 21053180; 21055077; 21087145; 21165435; 21185702; 21292323; 21434422; 21636625; 21842217; 21852236; 21900206; 21904836; 21921984; 21936966; 21989715; 21993316; 22072582; 22167619; 22180033; 22259188; 22561328; 22645453; 22677746; 22683538; 22699881; 22704671; 22715394; 22790458; 22843889; 22888637; 22890915; 22952184; 22964634; 23010849; 23063346; 23073788; 23152058; 23212700; 23261989; 23289525; 23518201; 23590304; 23721877; 23725507; 23748877; 23765060; 23781296; 23837478; 23975365; 24037914; 24039907; 24054539; 24058403; 24212762; 24323765; 24512906; 24563517; 24597264; 24634124; 24719327; 24817295; 24841661; 24887198; 2501828; 25033027; 25047527; 25283363; 25439478; 25497738; 25525879; 25550558; 25666858; 25670081; 25786472; 25866291; 25894370; 26112936; 26124081; 26125826; 26275098; 26355565; 26369242; 26446998; 26477504; 26545512; 26638075; 26658762; 26661784; 26662676; 26674569; 26685757; 26773925; 26782341; 26787049; 26823947; 26829742; 26881045; 26897098; 26970173; 26990426; 26991090; 27028814; 27067415; 27069153; 27100222; 27164132; 27188866; 27218102; 27229152; 27450956; 27592002; 27825163; 27914828; 27993878; 28011951; 28055018; 28070146; 28073131; 28087256; 28089078; 28141554; 28145855; 28174350; 28179340; 28222320; 28298473; 28322753; 28547970; 28587495; 28653098; 28696394; 28872562; 29187474; 29246792; 29411539; 29499564; 29543921; 29609868; 29980787; 30225256; 30256368; 30358222; 30515395; 30538220; 30632027; 31032363; 31340563; 31382611; 31512047; 31576926; 31765890; 31801023; 31844035; 31926619; 32203639; 32278283; 32306674; 32423796; 32735635; 32799270; 32877752; 32885455; 32917014; 33009206; 33070477; 33085656; 33098285; 33616746; 3457020; 34863990; 34997988; 35062064; 35361071; 6816802; 807573; 8428933; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,088 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16833; RHEA:16834; RHEA:50708; RHEA:50709 |
| Cross Reference Brenda | 1.11.1.9; |