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Literature summary for 1.8.1.10 extracted from

  • Ondarza, R.N.; Escamilla, E.; Gutierrez, J.; de la Chica, G.
    CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity (1974), Biochim. Biophys. Acta, 341, 162-171.
    View publication on PubMed
Search for more literature for 1.8.1.10

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
 CoA-glutathione at pH 5.75 and a fixed value of 110 nmol NADPH Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42500
-
 gel filtration, one protein with CoASSG reductase and GSSG reductase activities, EC 1.6.4.2 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
289fold purification Rattus norvegicus
not separated from GSSG reductase activity, EC 1.6.4.2 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA-glutathione + NADPH high substrate specificity Rattus norvegicus glutathione + CoA + NADP+
-
 ?
additional information no reduction of disulfides such as cystine, cystamine, panthetine, and insulin Rattus norvegicus ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADPH NADPH-dependent Rattus norvegicus