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Literature summary extracted from

  • Untucht-Grau, R.; Schirmer, R.H.; Schirmer, I.; Krauth-Siegel, R.L.
    Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain (1981), Eur. J. Biochem., 120, 407-419.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.7 52500
-
 2 * 52500 Homo sapiens

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.7 amino acid sequence analysis Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ substrate and cofactor binding site, three-dimensional structure Homo sapiens
a

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+
-
 r

Subunits

EC Number Subunits Comment Organism
1.8.1.7 dimer 2 * 52500 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 FAD amino acid sequence of FAD-binding domain Homo sapiens
1.8.1.7 FAD FAD enzyme Homo sapiens
1.8.1.7 NADPH
-
 Homo sapiens