Detail Information for IndEnz0018000736
IED ID IndEnz0018000736
Enzyme Type ID peroxidase000736
Protein Name Glutathione S-transferase Mu 2
EC 2.5.1.18
GST class-mu 2
GSTM2-2
Gene Name GSTM2 GST4
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 MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK
Enzyme Length 218
Uniprot Accession Number P28161
Absorption
Active Site
Activity Regulation
Binding Site BINDING 50; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P08010; BINDING 116; /note=Substrate; /evidence=ECO:0000250
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:16549767};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000305|PubMed:16549767}; 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. Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). {ECO:0000269|PubMed:16549767, ECO:0000269|PubMed:21046276}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Beta strand (8); Binding site (2); Chain (1); Domain (2); Helix (9); Modified residue (2); Mutagenesis (1); Natural variant (1); Region (4); Sequence conflict (3); Site (1); Turn (4)
Keywords 3D-structure;Alternative splicing;Cytoplasm;Direct protein sequencing;Lipid metabolism;Phosphoprotein;Reference proteome;Transferase
Interact With P46439
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue MOD_RES 27; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P08010; MOD_RES 44; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P08010
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (11)
Cross Reference PDB 1HNA; 1HNB; 1HNC; 1XW5; 1YKC; 2AB6; 2C4J; 2GTU; 3GTU; 3GUR; 5HWL;
Mapped Pubmed ID 10329152; 10587441; 10652317; 10783391; 11327815; 12042665; 12211029; 12486119; 12627223; 12871945; 14634838; 15725629; 16002077; 16081649; 16298388; 16548513; 17197702; 18007994; 18065725; 18308613; 18510611; 18551009; 19151192; 19168034; 19343046; 19696791; 19856098; 19859803; 19913121; 20083122; 20085333; 20200426; 20417188; 20485444; 20628086; 21106529; 21246532; 21268265; 21454564; 21455499; 21668448; 22522127; 23675469; 24399650; 24852519; 24965446; 27566576; 32574561; 33555546; 8203914; 8331657; 8431482; 9551553; 9761928; 9839448;
Motif
Gene Encoded By
Mass 25,745
Kinetics
Metal Binding
Rhea ID RHEA:16437; RHEA:16438; RHEA:50260; RHEA:50261
Cross Reference Brenda 2.5.1.18;