| IED ID | IndEnz0018000530 |
| Enzyme Type ID | peroxidase000530 |
| Protein Name |
Glutathione S-transferase A2 EC 2.5.1.18 GST class-alpha member 2 Glutathione S-transferase GT41A |
| Gene Name | Gsta2 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAGKPVLHYFNARGRMECIRWLLAAAGVEFEEKFIQSPEDLEKLKKDGNLMFDQVPMVEIDGMKLVQTRAILNYIATKYDLYGKDMKERALIDMYTEGILDLTEMIGQLVLCPPDQREAKTALAKDRTKNRYLPAFEKVLKSHGQDYLVGNRLTRVDVHLLELLLYVEELDASLLTPFPLLKAFKSRISSLPNVKKFLHPGSQRKPPLDAKQIEEARKVFKF |
| Enzyme Length | 222 |
| Uniprot Accession Number | P10648 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 9; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P13745; BINDING 45; /note=Glutathione; /evidence=ECO:0000305|PubMed:12549910 |
| 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:9606968};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000305|PubMed:9606968}; |
| DNA Binding | |
| EC Number | 2.5.1.18 |
| Enzyme Function | FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. {ECO:0000269|PubMed:9606968}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Binding site (2); Chain (1); Domain (2); Helix (13); Initiator methionine (1); Modified residue (2); Region (2); Sequence conflict (1); Turn (1) |
| Keywords | 3D-structure;Acetylation;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P30115; MOD_RES 4; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P30115 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1ML6; |
| Mapped Pubmed ID | 11217851; 11851347; 12466851; 14610273; 14681479; 15870285; 1728405; 1981995; 21554947; 23012479; 7774561; 7894162; 9268051; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,542 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 uM for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968}; Vmax=1295 nmol/min/mg enzyme for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968}; |
| Metal Binding | |
| Rhea ID | RHEA:16437; RHEA:16438 |
| Cross Reference Brenda |