Detail Information for IndEnz0018000174
IED ID IndEnz0018000174
Enzyme Type ID peroxidase000174
Protein Name Glutathione peroxidase 1
GPx-1
GSHPx-1
EC 1.11.1.9
Cellular glutathione peroxidase
Gene Name GPX1
Organism Oryctolagus cuniculus (Rabbit)
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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit)
Enzyme Sequence MCAARMAAAAQSVYSFSAHPLAGGEPVNLGSLRGKVLLIENVASLUGTTVRDYTQMNELQERLGPRALVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFQKCEVNGAKASPLFAFLREALPPPSDDPTALMTDPKFITWCPVCRNDVSWSFEKFLVGPDGVPVRRYSRRFPTIDIEPDIQALLSKGSGGA
Enzyme Length 200
Uniprot Accession Number P11909
Absorption
Active Site ACT_SITE 46
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.
Modified Residue MOD_RES 31; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041; MOD_RES 85; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 85; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 111; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 111; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 118; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 145; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 145; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P11352; MOD_RES 194; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04041
Post Translational Modification PTM: During periods of oxidative stress, Sec-46 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 21,883
Kinetics
Metal Binding
Rhea ID RHEA:16833; RHEA:16834; RHEA:50708; RHEA:50709
Cross Reference Brenda