IED Industry Enzyme Database

Detail Information for IndEnz0018000993
IED ID IndEnz0018000993
Enzyme Type ID peroxidase000993
Protein Name Glutathione S-transferase P
EC 2.5.1.18
GST class-pi
GSTP1-1
Gene Name GSTP1 FAEES3 GST3
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 MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ
Enzyme Length 210
Uniprot Accession Number P09211
Absorption
Active Site
Activity Regulation
Binding Site BINDING 8; /note="Glutathione"; /evidence="ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"; BINDING 14; /note="Glutathione"; /evidence="ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"; BINDING 39; /note="Glutathione"; /evidence="ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"; BINDING 45; /note="Glutathione"; /evidence="ECO:0000269|PubMed:1522586, ECO:0000269|PubMed:19396894, ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:9012673, ECO:0000269|PubMed:9245401, ECO:0000269|PubMed:9351803, ECO:0000269|PubMed:9398518"
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:0000269|PubMed:1540159, ECO:0000269|PubMed:1567427, ECO:0000269|PubMed:8433974};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000305}; 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:0000269|PubMed:9084911};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000305|PubMed:9084911}; 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:0000269|PubMed:9084911};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809; Evidence={ECO:0000305|PubMed:9084911}; 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:0000269|PubMed:9084911};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801; Evidence={ECO:0000305|PubMed:9084911}; 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:0000269|PubMed:21046276};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000305|PubMed:21046276};
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) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000269|PubMed:21046276, ECO:0000269|PubMed:21668448, ECO:0000269|PubMed:9084911}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Binding site (4); Chain (1); Domain (2); Helix (13); Initiator methionine (1); Modified residue (6); Mutagenesis (2); Natural variant (3); Region (2); Sequence conflict (1)
Keywords 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Lipid metabolism;Mitochondrion;Nucleus;Phosphoprotein;Reference proteome;Transferase
Interact With Q6UY14-3; Q92624; Q9BWT7; A8MQ03; Q5TD97; P49639; Q15323; Q14525; O76011; P78385; Q07627; Q8IUG1; P60409; P60411; Q9BYR8; Q9BYR6; Q3LI66; Q9P2M1; Q5JR59-3; Q7Z3S9; P0DPK4; P22735; Q12933; Q8N720
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19269317}. Mitochondrion {ECO:0000269|PubMed:19269317}. Nucleus {ECO:0000269|PubMed:19269317}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.
Modified Residue MOD_RES 4; /note=Phosphotyrosine; by EGFR; /evidence=ECO:0000269|PubMed:19254954; MOD_RES 62; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 103; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P19157; MOD_RES 116; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P19157; MOD_RES 128; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 199; /note=Phosphotyrosine; by EGFR; /evidence=ECO:0000269|PubMed:19254954
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (66)
Cross Reference PDB 10GS; 11GS; 12GS; 13GS; 14GS; 16GS; 17GS; 18GS; 19GS; 1AQV; 1AQW; 1AQX; 1EOG; 1EOH; 1GSS; 1KBN; 1LBK; 1MD3; 1MD4; 1PGT; 1PX6; 1PX7; 1ZGN; 20GS; 22GS; 2A2R; 2A2S; 2GSS; 2J9H; 2PGT; 3CSH; 3CSI; 3CSJ; 3DD3; 3DGQ; 3GSS; 3GUS; 3HJM; 3HJO; 3HKR; 3IE3; 3KM6; 3KMN; 3KMO; 3N9J; 3PGT; 4GSS; 4PGT; 5DAK; 5DAL; 5DCG; 5DDL; 5DJL; 5DJM; 5GSS; 5J41; 5JCW; 5L6X; 5X79; 6AP9; 6GSS; 6LLX; 6Y1E; 7GSS; 8GSS; 9GSS;
Mapped Pubmed ID 10329152; 10413721; 10450859; 10452896; 10587441; 10780269; 10783391; 10806136; 10856703; 10919500; 10970734; 11040079; 11044240; 11045797; 11059750; 11081456; 11086181; 11097238; 11131031; 11159743; 11169956; 11186133; 11186134; 11191882; 11291049; 11303592; 11307147; 11327815; 11389067; 11406608; 11408349; 11408954; 11434510; 11470996; 11511301; 11535247; 11535248; 11535253; 11550208; 11553769; 11562107; 11686891; 11692073; 11700265; 11739132; 11740339; 11751372; 11751440; 11757669; 11773866; 11783115; 11788897; 11796315; 11809677; 11844594; 11862479; 11895912; 11906705; 11912447; 11927838; 11943609; 11948486; 11956078; 11960994; 11967624; 11994713; 12010828; 12010858; 12019159; 12029283; 12036913; 12042665; 12072547; 12091121; 12112003; 12112555; 12127421; 12139976; 12148855; 12153964; 12153968; 12172391; 12172904; 12175548; 12189190; 12204870; 12210727; 12211029; 12241105; 12297838; 12359356; 12360105; 12376472; 12376511; 12397416; 12414796; 12419832; 12435115; 12439226; 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Motif
Gene Encoded By
Mass 23,356
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=395 uM for prostaglandin A2 (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:9084911}; KM=201 uM for prostaglandin J2 (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:9084911}; Vmax=267 nmol/min/mg enzyme for the formation of the glutathione-S-conjugate of prostaglandin A2 (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:9084911}; Vmax=105 nmol/min/mg enzyme for the formation of the glutathione-S-conjugate of prostaglandin J2 (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:9084911};
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;