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Literature summary for 1.8.5.1 extracted from

  • Washburn, M.P.; Wells, W.W.
    The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin) (1999), Biochemistry, 38, 268-274.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C25S has equivalent specificity constants for dehydroascorbate and GSH, but may have a different catalytic mechanism Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.32
-
dehydroascorbate glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin) Sus scrofa
0.51
-
dehydroascorbate glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant Sus scrofa
3.7
-
GSH glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin) Sus scrofa
5.2
-
GSH glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate catalytic mechanism Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSH + dehydroascorbate
-
Sus scrofa GSSG + ascorbate
-
?
additional information glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin) Sus scrofa ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Sus scrofa