| IED ID | IndEnz0018000353 |
| Enzyme Type ID | peroxidase000353 |
| Protein Name |
Glutathione S-transferase D2 EC 2.5.1.18 |
| Gene Name | GstD2 GSTD2-2 gstD21 CG4181 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MDFYYMPGGGGCRTVIMVAKALGLELNKKLLNTMEGEQLKPEFVKLNPQHTIPTLVDNGFSIWESRAIAVYLVEKYGKDDYLLPNDPKKRAVINQRLYFDMGTLYESFAKYYYPLFRTGKPGSDEDLKRIETAFGFLDTFLEGQEYVAGDQLTVADIAILSTVSTFEVSEFDFSKYSNVSRWYDNAKKVTPGWDENWEGLMAMKALFDARKLAAK |
| Enzyme Length | 215 |
| Uniprot Accession Number | Q9VG98 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| 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:22082028}; |
| 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 (PubMed:22082028). May be involved in detoxification (PubMed:22082028). {ECO:0000269|PubMed:22082028}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (5); Chain (1); Domain (2); Helix (11); Region (2); Turn (2) |
| Keywords | 3D-structure;Detoxification;Reference proteome;Transferase |
| Interact With | Q9VG92 |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5F0G; |
| Mapped Pubmed ID | 11157786; 11358508; 11583575; 12118001; 12443531; 14595091; 14612442; 15136717; 16814731; 16973896; 17098168; 17907271; 18039872; 18651915; 19237508; 19342413; 19348653; 19410610; 19667135; 20184862; 21264254; 22010830; 22296880; 22430022; 22479193; 22832276; 23071443; 23438069; 23861907; 23944235; 24099738; 24429422; 24439372; 24670639; 24865556; 25063457; 25193493; 25310450; 25347746; 25511696; 25682008; 26097463; 26162375; 26298685; 26383889; 26390919; 26452202; 26509186; 26801178; 27058248; 27068460; 27357258; 27794539; 28450373; 29324667; 29357349; 29515102; 29578047; 29679661; 30153653; 30665104; 30682390; 31481676; 31636947; 32284136; 32344153; 32468146; 32598400; 32664584; 32773682; 33109529; 33306674; 33349477; 34039988; 34066348; 34553686; 34662537; 7775439; 7961718; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,535 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.84 mM for glutathione {ECO:0000269|PubMed:22082028}; KM=0.81 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:22082028}; Vmax=0.53 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:22082028}; Vmax=0.50 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate {ECO:0000269|PubMed:22082028}; Vmax=0.013 umol/min/mg enzyme with phenethyl isothiocyanate as substrate {ECO:0000269|PubMed:22082028}; |
| Metal Binding | |
| Rhea ID | RHEA:16437 |
| Cross Reference Brenda |