Detail Information for IndEnz0018000004
IED ID IndEnz0018000004
Enzyme Type ID peroxidase000004
Protein Name Glutathione peroxidase 2
GPx-2
GSHPx-2
EC 1.11.1.9
Gastrointestinal glutathione peroxidase
Glutathione peroxidase-gastrointestinal
GPx-GI
GSHPx-GI
Glutathione peroxidase-related protein 2
GPRP-2
Gene Name GPX2
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 MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRFPRRLVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEPDIKRLLKVAI
Enzyme Length 190
Uniprot Accession Number P18283
Absorption
Active Site ACT_SITE 40
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; Evidence={ECO:0000269|PubMed:8428933};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62633; Evidence={ECO:0000269|PubMed:8428933}; 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:0000269|PubMed:8428933};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000269|PubMed:8428933}; CATALYTIC ACTIVITY: Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412, ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:64090; Evidence={ECO:0000269|PubMed:8428933};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413; Evidence={ECO:0000269|PubMed:8428933}; CATALYTIC ACTIVITY: Reaction=cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2O; Xref=Rhea:RHEA:69651, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:78673, ChEBI:CHEBI:131607; Evidence={ECO:0000269|PubMed:8428933};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652; Evidence={ECO:0000269|PubMed:8428933};
DNA Binding
EC Number 1.11.1.9
Enzyme Function FUNCTION: Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides (PubMed:8428933). Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors (PubMed:8428933). {ECO:0000269|PubMed:8428933}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (8); Chain (1); Helix (9); Natural variant (4); Non-standard residue (1); Sequence conflict (2); Turn (1)
Keywords 3D-structure;Cytoplasm;Oxidoreductase;Peroxidase;Reference proteome;Selenocysteine
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8428933}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2HE3;
Mapped Pubmed ID 10549853; 11115402; 11811519; 12751789; 15923610; 16446369; 16794261; 17277236; 17937616; 18056462; 18479189; 18483336; 18676680; 19047153; 19161995; 19170196; 19573080; 19625176; 19692168; 19773279; 19913121; 20200426; 20628086; 20813000; 21988832; 22683372; 22758632; 23934683; 24562575; 2501828; 25261240; 25813210; 27388201; 28453466; 28631563; 28635398; 28916653; 30652380; 31765890; 31774184; 32215178; 33622868; 34954079; 35193955; 6816802;
Motif
Gene Encoded By
Mass 21,954
Kinetics
Metal Binding
Rhea ID RHEA:62632; RHEA:62633; RHEA:16833; RHEA:16834; RHEA:69412; RHEA:69413; RHEA:69651; RHEA:69652
Cross Reference Brenda 1.11.1.9;