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Literature summary 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

Crystallization (Commentary)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.7 0.021
-
NADPH
-
Sus scrofa
1.8.1.7 0.076
-
GSSG
-
Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.7 59000
-
2 * 59000, SDS-PAGE Sus scrofa
1.8.1.7 103000
-
analytical ultracentrifugation Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.7
-
Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.7 erythrocyte
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.7 221
-
purified enzyme Sus scrofa

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.7 5
-
NADH + GSSG Sus scrofa
1.8.1.7 7
-
NADPH + GSSG Sus scrofa

Cofactor

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