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Literature summary for 1.18.1.2 extracted from
- Thermal inactivation of reduced ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli (2002), FEBS Lett., 529, 237-242.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | enzyme can be an electron source in biotechnological applications | Escherichia coli |
General Stability
| General Stability | Organism |
|---|---|
| binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, rapid thermal inactivation of reduced enzyme and drop of activity | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| oxidized ferredoxin + NADPH | Escherichia coli | ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH | reduced ferredoxin + NADP+ | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| soluble enzyme by ultracentrifugation, DEAE ion exchange chromatography, dialysis, and hydroxyapatite chromatography | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NADPH + H+ + oxidized 2,6-dichlorophenolindophenol | - |
Escherichia coli | NADP+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
| oxidized ferredoxin + NADPH | - |
Escherichia coli | reduced ferredoxin + NADP+ | - |
? | |
| oxidized ferredoxin + NADPH | ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH | Escherichia coli | reduced ferredoxin + NADP+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ferredoxin (flavodoxin):NADP+ oxidoreductase | - |
Escherichia coli |
| FNR | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | 40 | - |
Escherichia coli |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 43 | - |
Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
rapid thermal inactivation of reduced enzyme | Escherichia coli |
| 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 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | 9 | - |
Escherichia coli |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7.5 | reduced thermal inactivation rate at this pH-range | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | noncovalently bound | Escherichia coli | |
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