Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ferricyanide | activation, direct reduction by reductaseNAP in the presence of NADH in vitro | Pseudomonas sp. |
General Stability | Organism |
---|---|
purification of reductase leads to significant loss of flavin cofactor | Pseudomonas sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,10-phenanthroline | 10 mM, 63% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
4-chloromercuribenzoate | 0.0005 mM, 94% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
iodoacetate | 10 mM, 50% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
N-ethylmaleimide | 2 mM, 30% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
NaN3 | 40 mM, 46% inhibition of ferredoxinNAP reductase | Pseudomonas sp. |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Pseudomonas sp. | 5737 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | component A, i.e. NADH-ferredoxinNAP reductase, of the multienzyme system is an iron-containing flavoprotein containing 1.8 g-atoms Fe2+ and 2 g-atoms sulfur | Pseudomonas sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP | Pseudomonas sp. |
34900 | - |
ferredoxinNAP reductase, native PAGE | Pseudomonas sp. |
36000 | - |
1 * 36000, ferredoxinNAP reductase, SDS-PAGE | Pseudomonas sp. |
37000 | - |
ferredoxinNAP reductase, gel filtration | Pseudomonas sp. |
37100 | - |
ferredoxinNAP reductase, deduced from amino acid sequence | Pseudomonas sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
naphthalene + NADH + O2 | Pseudomonas sp. | three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase | (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
ferredoxinNAP reductase, Blue Sepharose, DEAE-cellulose | Pseudomonas sp. |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | proposed electron transport chain: NADH, ferredoxixinNAP reductase, ferredoxinNAP, terminal oxygenase ISPNAP | Pseudomonas sp. |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
397 | - |
cytochrome c reduction by ferredoxinNAP reductase | Pseudomonas sp. |
Storage Stability | Organism |
---|---|
-20°C, ferredoxinNAP reductase, 1 month, minimal loss of activity, prolonged storage leads to precipitation when preparation is heated above 5°C | Pseudomonas sp. |
0-5°C, ferredoxinNAP reductase, 5 days, 30% loss of activity | Pseudomonas sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
naphthalene + NADH + O2 | 3 component enzyme system consisting of ferredoxinNAP reductase, ferredoxinNAP and oxygenase ISPNAP, ferredoxinNAP reductase reduces: 2,6-dichlorophenolindophenol, ferricyanide, nitro blue tetrazolium and cytochrome c, in the presence of FAD ferredoxinNAP reductase transfers electrons to ferredoxin | Pseudomonas sp. | cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? | |
naphthalene + NADH + O2 | three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase | Pseudomonas sp. | (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 36000, ferredoxinNAP reductase, SDS-PAGE | Pseudomonas sp. |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
room temperature, ferredoxinNAP reductase, t1/2: 8 h | Pseudomonas sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
ferredoxin reductaseNAP, pI: 6.3 | Pseudomonas sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | 1 mol FAD/mol enzyme in flavin-reconstituted protein | Pseudomonas sp. | |
FAD | component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD | Pseudomonas sp. | |
FAD | addition enhances ferredoxinNAP reductase activity with all in vitro electron-acceptors, e.g. cytochrome c, 2,6-dichlorophenolindophenol, Nitroblue tetrazolium and ferricyanide | Pseudomonas sp. | |
FMN | requirement, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD, addition stimulates dioxygenase activity by 53% of FAD-stimulation | Pseudomonas sp. | |
NADH | - |
Pseudomonas sp. | |
NADPH | ferredoxinNAP reductase | Pseudomonas sp. | |
NADPH | can replace NADH with 39% | Pseudomonas sp. |