Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Application

EC Number Application Comment Organism
1.18.1.2 biotechnology enzyme can be an electron source in biotechnological applications Escherichia coli

General Stability

EC Number General Stability Organism
1.18.1.2 binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme Escherichia coli
1.19.1.1 binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme Escherichia coli
1.19.1.1 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information kinetics, rapid thermal inactivation of reduced enzyme and drop of activity Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 soluble
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 oxidized ferredoxin + NADPH Escherichia coli ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH reduced ferredoxin + NADP+
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.2 soluble enzyme by ultracentrifugation, DEAE ion exchange chromatography, dialysis, and hydroxyapatite chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
-
 Escherichia coli NADP+ + reduced 2,6-dichlorophenolindophenol
-
 ?
1.18.1.2 oxidized ferredoxin + NADPH
-
 Escherichia coli reduced ferredoxin + NADP+
-
 ?
1.18.1.2 oxidized ferredoxin + NADPH ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH Escherichia coli reduced ferredoxin + NADP+
-
 ?
1.19.1.1 reduced 2,6-dichlorophenolindophenol + NADP+
-
 Escherichia coli oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
 ?
1.19.1.1 reduced flavodoxin + NADP+
-
 Escherichia coli oxidized flavodoxin + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.18.1.2 monomer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin (flavodoxin):NADP+ oxidoreductase
-
 Escherichia coli
1.18.1.2 FNR
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.1.2 37 40
-
 Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.18.1.2 25 43
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.18.1.2 additional information
-
 rapid thermal inactivation of reduced enzyme Escherichia coli
1.18.1.2 37
-
 inactivation of the enzyme due to irreversible protein unfolding and dissociation of the FADH2 cofactor, slower process with binding of ferredoxin, FAD, or flavodoxin, best by riboflavin, overview Escherichia coli
1.19.1.1 37
-
 reduced FNR is subject to inactivation due to unfolding of the protein and dissociation of the FADH2 cofactor Escherichia coli
1.19.1.1 41
-
 melting temperature,reduced FNR in presence of dithiothreitol Escherichia coli
1.19.1.1 66
-
 melting temperature,oxidized FNR in presence of dithiothreitol Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 8.5 9
-
 Escherichia coli

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.18.1.2 6.5 7.5 reduced thermal inactivation rate at this pH-range Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD noncovalently bound Escherichia coli