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Literature summary for 1.18.1.2 extracted from

  • Pueyo, J.J.; Sancho, J.; Edmondson, D.E.; Gomez-Moreno, C.
    Preparation and properties of a cross-linked complex between ferredoxin-NADP+ reductase and flavodoxin (1989), Eur. J. Biochem., 183, 539-544.
    View publication on PubMed
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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
additional information
-
 additional information enzyme covalently cross-linked to flavodoxin Trichormus variabilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
-
 Trichormus variabilis

Organism

Organism UniProt Comment Textmining
Trichormus variabilis
-
-
-

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7
-
 NADPH NADPH cytochrome c reductase activity, flavodoxin Trichormus variabilis
100
-
 NADPH NADPH cytochrome c reductase activity, ferredoxin Trichormus variabilis
267
-
 NADPH diaphorase activity, FNR-flavodoxin complex Trichormus variabilis
517
-
 NADPH diaphorase activity Trichormus variabilis

Cofactor

Cofactor Comment Organism Structure
NADP+ reductase is covalently cross linked to Azotobacter vinelandii flavodoxin Trichormus variabilis