EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.18 | GSTD1 and GSTD10, genome organization and sequence comparison, expression in Escherichia coli strain BL21(DE3)pLysS | Drosophila melanogaster |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.18 | dmGSTD10 in apo- and glutathione-bound form, and dmGSTD1, hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, with 0.002 ml of reservoir solution16 and 23°C, X-ray diffraction structure determination and analysis, attempts to crystallize dmGSTD1 apo-form are unsuccessful due to its affinity toward glutathione ligand | Drosophila melanogaster |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.5.1.18 | 0.23 | - |
glutathione | GSTD1, pH and temperature not specified in the publication | Drosophila melanogaster |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.18 | RX + glutathione | Drosophila melanogaster | - |
HX + R-S-glutathione | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.18 | Drosophila melanogaster | - |
isozymes GSTD1 and GSTD10 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.18 | recombinant GSTD1 and GSTD10 from Escherichia coli strain BL21(DE3)pLysS by anion exchange and hydrophobic interaction chromatography | Drosophila melanogaster |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.5.1.18 | SCHNEIDER-2 cell | - |
Drosophila melanogaster | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.18 | RX + glutathione | - |
Drosophila melanogaster | HX + R-S-glutathione | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.18 | dimer | subunit dimerization is mainly formed by an electrostatic interaction and a distinctive lock-and-key clasp motif for Delta class GSTs, GSTD1 and GSTD10 structure, modeling, GST tertiary structures comparisons, overview | Drosophila melanogaster |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.18 | GSTD1 | - |
Drosophila melanogaster |
2.5.1.18 | GSTD10 | - |
Drosophila melanogaster |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.18 | evolution | the enzyme belongs to the glutathione transferase, GST, superfamily. Phylogenetic analysis shows, among the Delta class, GSTD1 and GSTD10 appear to be recently diverged transcripts with 86% amino acid sequence similarity | Drosophila melanogaster |