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Literature summary for 1.8.1.7 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
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Activating Compound

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

Crystallization (Commentary)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 relative activity and reaction velocity with diverse FAD analogues Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GSSG + NADPH
-
 Homo sapiens glutathione + NADP+
-
 r
additional information active with diverse FAD analogues, dependent on orientation of the cofactor Homo sapiens ?
-
 ?

Cofactor

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