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Literature summary for 1.19.1.1 extracted from

  • Jarrett, J.T.; Wan, J.T.
    Thermal inactivation of reduced ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli (2002), FEBS Lett., 529, 237-242.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.19.1.1

General Stability

General Stability Organism
binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme Escherichia coli
FNR reduced in the presence of NADPH is slowly inactivated under all conditions. Reactivity towards flavodoxin is lost most rapidly (kinact of 0.031 per min) with less than 10% of the original activity remaining after 30 min, reactivity towards ferredoxin is not as rapidly affected (kinact of 0.0065 per min) with 80% of the original activity remaining after 30 min Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced 2,6-dichlorophenolindophenol + NADP+
-
 Escherichia coli oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
 ?
reduced flavodoxin + NADP+
-
 Escherichia coli oxidized flavodoxin + NADPH + H+
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 reduced FNR is subject to inactivation due to unfolding of the protein and dissociation of the FADH2 cofactor Escherichia coli
41
-
 melting temperature,reduced FNR in presence of dithiothreitol Escherichia coli
66
-
 melting temperature,oxidized FNR in presence of dithiothreitol Escherichia coli