| IED ID | IndEnz0018001289 |
| Enzyme Type ID | peroxidase001289 |
| Protein Name |
Microsomal glutathione S-transferase 1 Microsomal GST-1 EC 2.5.1.18 Microsomal GST-I |
| Gene Name | MGST1 GST12 |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MADLTELMKNEVFMAFASYATIVLSKMMFMSTATAFYRLTRKVFANPEDCSSFGKGENAKKYLRTDERVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTAILHFRLFVGARIYHTIAYLTPLPQPNRGLAFFLGYGVTLSMAYRLLKSRLYL |
| Enzyme Length | 155 |
| Uniprot Accession Number | P79382 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide. Activation also occurs via nitration of Tyr-93 by peroxynitrite (By similarity). {ECO:0000250}. |
| Binding Site | BINDING 38; /note=Glutathione; /evidence=ECO:0000250; BINDING 73; /note=Glutathione; /evidence=ECO:0000250; BINDING 74; /note=Glutathione; /evidence=ECO:0000250; BINDING 76; /note=Glutathione; /evidence=ECO:0000250; BINDING 81; /note=Glutathione; /evidence=ECO:0000250; BINDING 121; /note=Glutathione; /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; |
| 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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (6); Chain (1); Modified residue (3); Site (1); Topological domain (5); Transmembrane (4) |
| Keywords | Acetylation;Endoplasmic reticulum;Membrane;Microsome;Mitochondrion;Mitochondrion outer membrane;Nitration;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. |
| 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 |
| Post Translational Modification | PTM: Peroxynitrite induces nitration at Tyr-93 which activates the enzyme. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 17,650 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16437 |
| Cross Reference Brenda |