Detail Information for IndEnz0018000737
IED ID IndEnz0018000737
Enzyme Type ID peroxidase000737
Protein Name Glutathione S-transferase P 1
Gst P1
EC 2.5.1.18
GST YF-YF
GST class-pi
GST-piB
Preadipocyte growth factor
Gene Name Gstp1 Gstpib
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 MPPYTIVYFPVRGRCEAMRMLLADQGQSWKEEVVTIDTWMQGLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKNQREAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVKALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLLIHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVNRPINGNGKQ
Enzyme Length 210
Uniprot Accession Number P19157
Absorption
Active Site
Activity Regulation
Binding Site BINDING 8; /note=Glutathione; /evidence=ECO:0000305|PubMed:8145243; BINDING 14; /note=Glutathione; /evidence=ECO:0000305|PubMed:8145243; BINDING 39; /note=Glutathione; /evidence=ECO:0000305|PubMed:8145243; BINDING 45; /note=Glutathione; /evidence=ECO:0000305|PubMed:8145243
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133772; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133769; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000250|UniProtKB:P09211};
DNA Binding
EC Number 2.5.1.18
Enzyme Function FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000250|UniProtKB:P09211}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (9); Binding site (4); Chain (1); Domain (2); Helix (12); Initiator methionine (1); Modified residue (5); Region (2); Turn (1)
Keywords 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Lipid metabolism;Mitochondrion;Nucleus;Phosphoprotein;Reference proteome;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}.
Modified Residue MOD_RES 4; /note=Phosphotyrosine; by EGFR; /evidence=ECO:0000250|UniProtKB:P09211; MOD_RES 62; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P09211; MOD_RES 103; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 116; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 128; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P09211
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (10)
Cross Reference PDB 1BAY; 1GLP; 1GLQ; 1GSY; 1GTI; 2GLR; 2OA7; 2OAC; 2OAD; 3O76;
Mapped Pubmed ID 10945608; 11058152; 11279197; 11408560; 12023900; 12225863; 12646564; 14517554; 14610273; 14681479; 14684749; 15386426; 16023107; 16160063; 16374777; 16399382; 16602821; 16615898; 17267597; 17909032; 18268004; 18349876; 18787219; 18792812; 18799693; 18962899; 18990698; 19269317; 19270193; 19455133; 19718438; 19739253; 19834914; 19915149; 19935654; 20404090; 20538586; 21134126; 21267068; 21748757; 21751364; 21975931; 22022436; 22084240; 22627280; 22751926; 22828627; 22956844; 23129554; 23164639; 23237955; 23647087; 24664677; 25216273; 25590808; 25868843; 25891661; 26169370; 26361746; 26838680; 27058114; 27086966; 29374060; 29520271; 29732603; 30153066; 30290218; 31299423; 31515511; 32320793; 32719131; 33437989; 34624602; 8584275; 9560266; 9677344; 9730611;
Motif
Gene Encoded By
Mass 23,609
Kinetics
Metal Binding
Rhea ID RHEA:16437; RHEA:16438; RHEA:50804; RHEA:50805; RHEA:50808; RHEA:50809; RHEA:50800; RHEA:50801; RHEA:50260; RHEA:50261
Cross Reference Brenda 2.5.1.18;