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Literature summary extracted from

  • Worthington, D.J.; Rosemeyer, M.A.
    Glutathione reductase from human erythrocytes. Molecular weight, subunit composition and aggregation properties (1975), Eur. J. Biochem., 60, 459-466.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.7 50000
-
2 * 50000, SDS-PAGE Homo sapiens
1.8.1.7 96000
-
apoenzyme without FAD, sedimentation equilibrium Homo sapiens
1.8.1.7 100000
-
sedimentation equilibrium Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.7 erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.8.1.7 dimer 2 * 50000, SDS-PAGE Homo sapiens
1.8.1.7 More in absence of thiols, glutathione reductase shows a tendency to form tetramers and larger aggregates, catalytically active Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 FAD FAD enzyme Homo sapiens
1.8.1.7 NADPH
-
Homo sapiens