Detail Information for IndEnz0018001135
IED ID IndEnz0018001135
Enzyme Type ID peroxidase001135
Protein Name Glutathione peroxidase 1
GPx-1
GSHPx-1
EC 1.11.1.9
Cellular glutathione peroxidase
Gene Name GPX1
Organism Hylobates lar (Common gibbon) (White-handed gibbon)
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) Hylobatidae (gibbons) Hylobates Hylobates lar (Common gibbon) (White-handed gibbon)
Enzyme Sequence MCAARLAAAAAQSVYAFSARPLTGGEPVSLGSLRGKILLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA
Enzyme Length 201
Uniprot Accession Number Q4AEI2
Absorption
Active Site ACT_SITE 47; /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;Selenocysteine
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue MOD_RES 32; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 86; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 86; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 112; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 112; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 146; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 146; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 195; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 199; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P07203
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:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 21,990
Kinetics
Metal Binding
Rhea ID RHEA:16833; RHEA:16834; RHEA:50708; RHEA:50709
Cross Reference Brenda