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Literature summary extracted from

  • Krauth-Siegel, R.L.; Schirmer, R.H.; Ghisla, S.
    FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure (1985), Eur. J. Biochem., 148, 335-344.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.7 FAD analogues properties of glutathione reductase reconstituted with FAD analogues Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.7 binding structure of diverse FAD analogues to the apoenzyme Homo sapiens

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ mechanism Homo sapiens
a
1.8.1.7 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ cofactor binding of glutathione reductase with FAD analogues, reconstitution Homo sapiens
a

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 additional information
-
 relative activity and reaction velocity with diverse FAD analogues 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
1.8.1.7 additional information active with diverse FAD analogues, dependent on orientation of the cofactor Homo sapiens ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 FAD properties of glutathione reductase reconstituted with FAD analogues Homo sapiens
1.8.1.7 FAD FAD enzyme Homo sapiens
1.8.1.7 FAD activity with diverse FAD analogues Homo sapiens
1.8.1.7 NADPH
-
 Homo sapiens