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Literature summary extracted from

  • Sancho, J.; Peleato, M.L.; Gomez-Moreno, C.; Edmondson, D.E.
    Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacteria Anabaena variabilis (1988), Arch. Biochem. Biophys., 260, 200-207.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information Km value increases with pH Trichormus variabilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.2 36000
-
 at least 5 molecular forms Trichormus variabilis

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Trichormus variabilis
-
 cyanobacterium
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 NADPH + oxidized ferredoxin
-
 Trichormus variabilis NADP+ + reduced ferredoxin
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 105
-
 NADPH NADPH-dichlorophenol indophenol diaphorase activity Trichormus variabilis
1.18.1.2 233
-
 NADPH NADPH-ferredoxin-cytochrome c reductase activity Trichormus variabilis
1.18.1.2 517
-
 NADPH NADPH-ferricyanide diaphorase activity Trichormus variabilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD flavoprotein Trichormus variabilis