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Literature summary for 1.18.1.2 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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Trichormus variabilis
-
cyanobacterium
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Trichormus variabilis