EC Number | Application | Comment | Organism |
---|---|---|---|
1.18.1.2 | biotechnology | enzyme can be an electron source in biotechnological applications | Escherichia coli |
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 |
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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.18.1.2 | soluble | - |
Escherichia coli | - |
- |
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+ | - |
? |
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 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.18.1.2 | soluble enzyme by ultracentrifugation, DEAE ion exchange chromatography, dialysis, and hydroxyapatite chromatography | Escherichia coli |
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+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.18.1.2 | monomer | - |
Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.18.1.2 | ferredoxin (flavodoxin):NADP+ oxidoreductase | - |
Escherichia coli |
1.18.1.2 | FNR | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.18.1.2 | 37 | 40 | - |
Escherichia coli |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.18.1.2 | 25 | 43 | - |
Escherichia coli |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.18.1.2 | 8.5 | 9 | - |
Escherichia coli |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.18.1.2 | FAD | noncovalently bound | Escherichia coli |