| IED ID | IndEnz0018001295 |
| Enzyme Type ID | peroxidase001295 |
| Protein Name |
Microsomal glutathione S-transferase 2 Microsomal GST-2 EC 2.5.1.18 Glutathione peroxidase MGST2 EC 1.11.1.- Leukotriene C4 synthase MGST2 EC 4.4.1.20 Microsomal glutathione S-transferase II Microsomal GST-II |
| Gene Name | MGST2 GST2 |
| 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 | MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFYPIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTLLGALGIANSFLDEYLDLNIAKKLRRQF |
| Enzyme Length | 147 |
| Uniprot Accession Number | Q99735 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Each monomer can bind on GSH molecule but only one subunit is catalytically active. {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:26066610}. |
| Binding Site | |
| 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:23409838, ECO:0000269|PubMed:26066610, ECO:0000269|PubMed:8703034}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:8703034}; CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000269|PubMed:11322876, ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:26656251, ECO:0000269|PubMed:8703034};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17618; Evidence={ECO:0000305|PubMed:23409838, ECO:0000305|PubMed:26656251}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:9278457}; |
| DNA Binding | |
| EC Number | 2.5.1.18; 1.11.1.-; 4.4.1.20 |
| Enzyme Function | FUNCTION: Catalyzes several different glutathione-dependent reactions (PubMed:8703034, PubMed:9278457, PubMed:23409838, PubMed:26656251, PubMed:26066610). Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE (PubMed:9278457, PubMed:23409838). Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB) (PubMed:23409838, PubMed:8703034). Catalyzes also the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4 (LTC4) (PubMed:23409838, PubMed:26656251). Involved in oxidative DNA damage induced by ER stress and anticancer agents by activating LTC4 biosynthetic machinery in nonimmune cells (PubMed:26656251). {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:26066610, ECO:0000269|PubMed:26656251, ECO:0000269|PubMed:8703034, ECO:0000269|PubMed:9278457}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Helix (5); Natural variant (1); Transmembrane (3) |
| Keywords | 3D-structure;Alternative splicing;Endoplasmic reticulum;Leukotriene biosynthesis;Lipid metabolism;Lyase;Membrane;Microsome;Oxidoreductase;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
| Interact With | P78348; Q9HD36; Q92843; P16619; Q86T13; O43889-2; Q96BA8; Q4LDR2; Q96LL9; Q96F15; P48165; Q8TED1; Itself; P26678; Q96T60; Q96IW7; O75396; Q16585; Q9UNK0; Q9NRX6; Q6UWW9; Q5BVD1; Q15836 |
| Induction | INDUCTION: Upon ER stress with brefeldin A or with tunicamycin, MGST2 is down-regulated, in several non-haematopoietic cell types, during the early, protective phase of the unfolded protein response (UPR), and up-regulated at the late, death-promoting phase of the unfolded protein response (UPR). {ECO:0000269|PubMed:26656251}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8703034}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:8703034}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 6SSR; 6SSS; 6SSU; 6SSW; |
| Mapped Pubmed ID | 11904223; 16498398; 16773312; 19343046; 20379614; 25609649; 3372534; 33741927; 8812420; |
| Motif | |
| Gene Encoded By | |
| Mass | 16,621 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (5-HPETE) {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:9278457}; KM=28 uM for leukotriene A4 {ECO:0000269|PubMed:11322876}; KM=40 uM for leukotriene A4 {ECO:0000269|PubMed:23409838}; Note=kcat is 0.6 sec(-1) for leukotriene A4 as substrate (PubMed:23409838). kcat is 14.3 sec(-1) for 1-chloro-2,4-dinitrobenzene as substrate (PubMed:23409838). kcat is 0.1 sec(-1) for 5-HPETE as substrate (PubMed:23409838). {ECO:0000269|PubMed:23409838}; |
| Metal Binding | |
| Rhea ID | RHEA:16437; RHEA:51220; RHEA:17617; RHEA:17618; RHEA:48620 |
| Cross Reference Brenda |