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Literature summary for 1.6.2.4 extracted from

  • Tryon, E.; Cress, M.C.; Hamada, M.; Kuby, S.A.
    Studies on NADPH-cytochrome c reductase I: Isolation and several properties of the crystalline enzyme from ale yeast (1979), Arch. Biochem. Biophys., 197, 104-118.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate) in absence of FAD or NADPH Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65000 68000 sedimentation equilibrium centrifugation, values depending on pH Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
150
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADPH additional electron acceptor: 2,6-dichlorophenolindophenol Saccharomyces cerevisiae 2 ferrocytochrome c + NADP+ + H+
-
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Subunits

Subunits Comment Organism
dimer 2 * 34300-40000, SDS-PAGE, sedimentation equilibrium centrifugation after treatment with guanidine-HCl Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
FAD and NADPH: protection against thermal inactivation Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol per subunit Saccharomyces cerevisiae
FMN
-
Saccharomyces cerevisiae