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Literature summary for 1.8.5.1 extracted from

  • Maellaro, E.; Del Bello, B.; Sugherini, L.; Comporti, M.; Casini, A.F.
    Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver (1997), Methods Enzymol., 279, 30-35.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.245
-
dehydroascorbate
-
Rattus norvegicus
2.8
-
GSH
-
Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
x * 31000, SDS-PAGE Rattus norvegicus
48700
-
gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSH + dehydroascorbate
-
Rattus norvegicus GSSG + ascorbate
-
?
GSH + isodehydroascorbate
-
Rattus norvegicus GSSG + isoascorbate
-
?
L-acetylcysteine + dehydroascorbate 4% of the activity with GSH Rattus norvegicus N,N'-diacetyl-L-cystine + ascorbate
-
?
L-Cys + dehydroascorbate 8% of the activity with GSH Rattus norvegicus ? + ascorbate
-
?

Subunits

Subunits Comment Organism
? x * 31000, SDS-PAGE Rattus norvegicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
5 min, 50% loss of activity Rattus norvegicus
75
-
5 min, 90% loss of activity Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
Rattus norvegicus