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Literature summary for 1.8.1.7 extracted from

  • Boggaram, V.; Brobjer, T.; Larson, K.; Mannervik, B.
    Purification of glutathione reductase from porcine erythrocytes by the use of affinity chromatography on 2,5-ADP-Sepharose 4B and crystallization of the enzyme (1979), Anal. Biochem., 98, 335-340.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop method at 22°C, size of crystals varies with ammonium sulfate concentration Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.021
-
 NADPH
-
 Sus scrofa
0.076
-
 GSSG
-
 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
 2 * 59000, SDS-PAGE Sus scrofa
103000
-
 analytical ultracentrifugation Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
221
-
 purified enzyme Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSSG + NADPH
-
 Sus scrofa glutathione + NADP+
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 59000, SDS-PAGE Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 NADH + GSSG Sus scrofa
7
-
 NADPH + GSSG Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD 2 mol of FAD per mol of enzyme Sus scrofa
FAD FAD enzyme Sus scrofa
NADH activity relative to NADPH: 0.5% Sus scrofa
NADPH best electron donor Sus scrofa