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Literature summary for 2.5.1.18 extracted from

  • Wongsantichon, J.; Yuvaniyama, J.; Ketterman, A.J.
    Crystallization and preliminary X-ray crystallographic analysis of a highly stable mutant V107A of glutathione transferase from Anopheles dirus in complex with glutathione (2006), Acta Crystallogr. Sect. F, 62, 310-312.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of GST adgstD4-4 mutant V107A in Escherichia coli strain BL21(DE3) Anopheles dirus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant GST adgstD4-4 mutant V107A, hanging drop vapour diffusion method, 0.002 ml of 9 mg/ml protein in 50 mM Tris–HCl, pH 7.5, 10 mM DTT, and 10 mM glutathione, are mixed with 0.002 ml of reservoir solution containing 0.1 M imidazole, pH 7.0, 0.35 M ammonium acetate, and 32% PEG 4000, 1 week, 22°C, X-ray diffraction structure determination and analysis at Anopheles dirus

Protein Variants

Protein Variants Comment Organism
V107A site-directed mutagenesis, highly stable enzyme mutant Anopheles dirus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Anopheles dirus the enzyme is involved in phase II detoxication processes by conjugation of a thiol group from reduced glutathione to an electrophilic centre of diverse xenobiotic compounds, producing less reactive and more polar substances in order to facilitate elimination from cells ?
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?

Organism

Organism UniProt Comment Textmining
Anopheles dirus
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GST adgstD4-4
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Purification (Commentary)

Purification (Comment) Organism
recombinant GST adgstD4-4 mutant V107A from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography Anopheles dirus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is involved in phase II detoxication processes by conjugation of a thiol group from reduced glutathione to an electrophilic centre of diverse xenobiotic compounds, producing less reactive and more polar substances in order to facilitate elimination from cells Anopheles dirus ?
-
?

Subunits

Subunits Comment Organism
More structural model of the wild-type GST adgstD4-4 shows that Val107 is located in the subunit-interface region of the dimeric GST, forming part of an intersubunit lock-and key clasp motif Anopheles dirus

Synonyms

Synonyms Comment Organism
GST adgstD4-4
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Anopheles dirus