| IED ID | IndEnz0018000621 |
| Enzyme Type ID | peroxidase000621 |
| Protein Name |
Microsomal glutathione S-transferase 1 Microsomal GST-1 EC 2.5.1.18 Microsomal GST-I |
| Gene Name | Mgst1 Gst12 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MADLKQLMDNEVLMAFTSYATIILAKMMFLSSATAFQRLTNKVFANPEDCAGFGKGENAKKFLRTDEKVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTALIHFRIFVGARIYHTIAYLTPLPQPNRGLAFFVGYGVTLSMAYRLLRSRLYL |
| Enzyme Length | 155 |
| Uniprot Accession Number | P08011 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide, except in the testis. Activation also occurs via nitration of Tyr-93 by peroxynitrite. {ECO:0000269|PubMed:16314419}. |
| Binding Site | BINDING 38; /note=Glutathione; /evidence=ECO:0000269|PubMed:16806268; BINDING 73; /note=Glutathione; /evidence=ECO:0000269|PubMed:16806268; BINDING 74; /note=Glutathione; /evidence=ECO:0000269|PubMed:16806268; BINDING 76; /note=Glutathione; /evidence=ECO:0000269|PubMed:16806268; BINDING 81; /note=Glutathione; /evidence=ECO:0000269|PubMed:16806268; BINDING 121; /note=Glutathione; /evidence=ECO:0000269|PubMed:16806268 |
| 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; |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Helix (8); Initiator methionine (1); Modified residue (4); Mutagenesis (2); Sequence conflict (7); Site (1); Topological domain (5); Transmembrane (4); Turn (1) |
| Keywords | 3D-structure;Acetylation;Direct protein sequencing;Endoplasmic reticulum;Membrane;Microsome;Mitochondrion;Mitochondrion outer membrane;Nitration;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome. Mitochondrion outer membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. |
| Modified Residue | MOD_RES 42; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91VS7; MOD_RES 55; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91VS7; MOD_RES 60; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91VS7; MOD_RES 93; /note=3'-nitrotyrosine; /evidence=ECO:0000269|PubMed:16314419 |
| Post Translational Modification | PTM: Peroxynitrite induces nitration at Tyr-93 which activates the enzyme. {ECO:0000269|PubMed:16314419}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (3) |
| Cross Reference PDB | 2H8A; 5I9K; 5IA9; |
| Mapped Pubmed ID | 14561759; 14726533; 15149725; 15236595; 16385473; 16899233; 17571305; 18634816; 19111564; 21216258; 21851097; 24419913; 28801553; 7173206; 9010624; |
| Motif | |
| Gene Encoded By | |
| Mass | 17,472 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16437 |
| Cross Reference Brenda | 2.5.1.18; |