Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.18 extracted from

  • Wongsantichon, J.; Robinson, R.C.; Ketterman, A.J.
    Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding (2012), Arch. Biochem. Biophys., 521, 77-83.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
GSTD1 and GSTD10, genome organization and sequence comparison, expression in Escherichia coli strain BL21(DE3)pLysS Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment) Organism
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
glutathione GSTD1, pH and temperature not specified in the publication Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RX + glutathione Drosophila melanogaster
-
HX + R-S-glutathione
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
isozymes GSTD1 and GSTD10
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GSTD1 and GSTD10 from Escherichia coli strain BL21(DE3)pLysS by anion exchange and hydrophobic interaction chromatography Drosophila melanogaster

Source Tissue

Source Tissue Comment Organism Textmining
SCHNEIDER-2 cell
-
Drosophila melanogaster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RX + glutathione
-
Drosophila melanogaster HX + R-S-glutathione
-
?

Subunits

Subunits Comment Organism
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

Synonyms

Synonyms Comment Organism
GSTD1
-
Drosophila melanogaster
GSTD10
-
Drosophila melanogaster

General Information

General Information Comment Organism
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