EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.12.12 | ferricyanide | activation, direct reduction by reductaseNAP in the presence of NADH in vitro | Pseudomonas sp. |
EC Number | General Stability | Organism |
---|---|---|
1.14.12.12 | purification of reductase leads to significant loss of flavin cofactor | Pseudomonas sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.12.12 | 1,10-phenanthroline | 10 mM, 63% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
1.14.12.12 | 4-chloromercuribenzoate | 0.0005 mM, 94% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
1.14.12.12 | iodoacetate | 10 mM, 50% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
1.14.12.12 | N-ethylmaleimide | 2 mM, 30% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
1.14.12.12 | NaN3 | 40 mM, 46% inhibition of ferredoxinNAP reductase | Pseudomonas sp. | |
1.18.1.3 | 1,10-phenanthroline | 10 mM, 30% inhibition | Pseudomonas sp. | |
1.18.1.3 | iodoacetate | 10 mM, 50% inhibition | Pseudomonas sp. | |
1.18.1.3 | NEM | 10 mM, 67% inhibition | Pseudomonas sp. | |
1.18.1.3 | PCMB | 0.0005 mM, 94% inhibition | Pseudomonas sp. | |
1.18.1.3 | Sodium azide | 40 mM, 46% inhibition | Pseudomonas sp. | |
1.18.1.7 | iodoacetate | 50% inhibition at 10 mM | Pseudomonas putida | |
1.18.1.7 | N-ethylmaleimide | 67% inhibition at 10 mM | Pseudomonas putida | |
1.18.1.7 | o-phenanthroline | 63% inhibition at 10 mM | Pseudomonas putida | |
1.18.1.7 | p-chloromercuribenzoate | 94% inhibition at 0.0005 mM | Pseudomonas putida | |
1.18.1.7 | Sodium azide | 46% inhibition at 40 mM | Pseudomonas putida |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.12.12 | cytoplasm | - |
Pseudomonas sp. | 5737 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.12.12 | 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. | |
1.18.1.3 | Iron | iron-sulfur flavoprotein, protein contains 1.8 gatom of iron and 2.0 gatom of acid-labile sulfur | Pseudomonas sp. | |
1.18.1.7 | Iron | the purified protein contains 1.8 g atoms of iron | Pseudomonas putida |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.12.12 | 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. |
1.14.12.12 | 34900 | - |
ferredoxinNAP reductase, native PAGE | Pseudomonas sp. |
1.14.12.12 | 36000 | - |
1 * 36000, ferredoxinNAP reductase, SDS-PAGE | Pseudomonas sp. |
1.14.12.12 | 37000 | - |
ferredoxinNAP reductase, gel filtration | Pseudomonas sp. |
1.14.12.12 | 37100 | - |
ferredoxinNAP reductase, deduced from amino acid sequence | Pseudomonas sp. |
1.18.1.3 | 34900 | - |
non-denaturing PAGE | Pseudomonas sp. |
1.18.1.3 | 36000 | - |
1 * 36000, SDS-PAGE | Pseudomonas sp. |
1.18.1.3 | 37000 | - |
gel filtration | Pseudomonas sp. |
1.18.1.7 | 36000 | - |
1 * 36000, SDS-PAGE | Pseudomonas putida |
1.18.1.7 | 37000 | - |
gel filtration | Pseudomonas putida |
1.18.1.7 | 37104 | - |
1 * 37104, calculated from amino acid sequence | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.12.12 | 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+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.12.12 | Pseudomonas sp. | - |
- |
- |
1.18.1.3 | Pseudomonas sp. | - |
- |
- |
1.18.1.3 | Pseudomonas sp. | - |
NADH-ferredoxinNAP reductase component of naphthalene dioxygenase | - |
1.18.1.3 | Pseudomonas sp. NCIB 9816 | - |
- |
- |
1.18.1.7 | Pseudomonas putida | Q52126 | - |
- |
1.18.1.7 | Pseudomonas putida NCIB 9816 | Q52126 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.12.12 | ferredoxinNAP reductase, Blue Sepharose, DEAE-cellulose | Pseudomonas sp. |
1.18.1.3 | NADH-ferredoxinNAP reductase component of naphthalene dioxygenase | Pseudomonas sp. |
1.18.1.7 | Sepharose CL-6B column chromatography and DEAE-cellulose column chromatography | Pseudomonas putida |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.12.12 | 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. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.14.12.12 | 397 | - |
cytochrome c reduction by ferredoxinNAP reductase | Pseudomonas sp. |
1.18.1.3 | 397 | - |
- |
Pseudomonas sp. |
1.18.1.7 | 397 | - |
purified enzyme, pH and temperature not specified in the publication | Pseudomonas putida |
EC Number | Storage Stability | Organism |
---|---|---|
1.14.12.12 | -20°C, ferredoxinNAP reductase, 1 month, minimal loss of activity, prolonged storage leads to precipitation when preparation is heated above 5°C | Pseudomonas sp. |
1.14.12.12 | 0-5°C, ferredoxinNAP reductase, 5 days, 30% loss of activity | Pseudomonas sp. |
1.18.1.3 | -20°C, 1 month, minimal loss of activity | Pseudomonas sp. |
1.18.1.3 | 0-5°C, 30% loss of activity after 5 days | Pseudomonas sp. |
1.18.1.7 | -20°C, purified enzyme, 1 month, minimal loss of activity | Pseudomonas putida |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.12.12 | 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+ | - |
? | |
1.14.12.12 | 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+ | - |
? | |
1.18.1.3 | 2 ferricyanide + NADH | - |
Pseudomonas sp. | 2 ferrocyanide + NAD+ + H+ | - |
? | |
1.18.1.3 | 2 ferricyanide + NADH | - |
Pseudomonas sp. NCIB 9816 | 2 ferrocyanide + NAD+ + H+ | - |
? | |
1.18.1.3 | 2 ferricytochrome c + NADH | - |
Pseudomonas sp. | 2 ferrocytochrome c + NAD+ + H+ | - |
? | |
1.18.1.3 | 2 ferricytochrome c + NADH | - |
Pseudomonas sp. NCIB 9816 | 2 ferrocytochrome c + NAD+ + H+ | - |
? | |
1.18.1.3 | NADH + oxidized 2,6-dichlorophenolindophenol + H+ | - |
Pseudomonas sp. | NAD+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
1.18.1.3 | NADH + oxidized 2,6-dichlorophenolindophenol + H+ | - |
Pseudomonas sp. NCIB 9816 | NAD+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
1.18.1.3 | NADH + oxidized nitro blue tetrazolium + H+ | - |
Pseudomonas sp. | NAD+ + reduced nitro blue tetrazolium | - |
? | |
1.18.1.3 | NADH + oxidized nitro blue tetrazolium + H+ | - |
Pseudomonas sp. NCIB 9816 | NAD+ + reduced nitro blue tetrazolium | - |
? | |
1.18.1.3 | NADPH + oxidized cytochrome c | 39% of the activity with NADH | Pseudomonas sp. | NADP+ + reduced cytochrome c | - |
? | |
1.18.1.3 | NADPH + oxidized cytochrome c | 39% of the activity with NADH | Pseudomonas sp. NCIB 9816 | NADP+ + reduced cytochrome c | - |
? | |
1.18.1.7 | 2 ferricyanide + NADH | best substrate | Pseudomonas putida | 2 ferrocyanide + NAD+ + H+ | - |
? | |
1.18.1.7 | 2 ferricyanide + NADH | best substrate | Pseudomonas putida NCIB 9816 | 2 ferrocyanide + NAD+ + H+ | - |
? | |
1.18.1.7 | 2 ferricytochrome c + NADH | - |
Pseudomonas putida | 2 ferrocytochrome c + NAD+ + H+ | - |
? | |
1.18.1.7 | 2 ferricytochrome c + NADH | - |
Pseudomonas putida NCIB 9816 | 2 ferrocytochrome c + NAD+ + H+ | - |
? | |
1.18.1.7 | NADH + H+ + oxidized 2,6-dichlorophenolindophenol | - |
Pseudomonas putida | NAD+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
1.18.1.7 | NADH + H+ + oxidized 2,6-dichlorophenolindophenol | - |
Pseudomonas putida NCIB 9816 | NAD+ + reduced 2,6-dichlorophenolindophenol | - |
? | |
1.18.1.7 | oxidized cytochrome c + NADPH | NADPH is also effective as an electron donor but yields only 39% of the activity obtained with NADH in the cytochrome c reductase assay | Pseudomonas putida | reduced cytochrome c + NADP+ + H+ | - |
? | |
1.18.1.7 | oxidized cytochrome c + NADPH | NADPH is also effective as an electron donor but yields only 39% of the activity obtained with NADH in the cytochrome c reductase assay | Pseudomonas putida NCIB 9816 | reduced cytochrome c + NADP+ + H+ | - |
? | |
1.18.1.7 | oxidized Nitro Blue tetrazolium + NADH | - |
Pseudomonas putida | reduced Nitro Blue tetrazolium + NAD+ + H+ | - |
? | |
1.18.1.7 | oxidized Nitro Blue tetrazolium + NADH | - |
Pseudomonas putida NCIB 9816 | reduced Nitro Blue tetrazolium + NAD+ + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.12.12 | monomer | 1 * 36000, ferredoxinNAP reductase, SDS-PAGE | Pseudomonas sp. |
1.18.1.3 | monomer | 1 * 36000, SDS-PAGE | Pseudomonas sp. |
1.18.1.7 | monomer | 1 * 36000, SDS-PAGE | Pseudomonas putida |
1.18.1.7 | monomer | 1 * 37104, calculated from amino acid sequence | Pseudomonas putida |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.18.1.3 | NADH-ferredoxinNAP reductase | component of naphthalene dioxygenase multicomponent enzyme system | Pseudomonas sp. |
1.18.1.7 | NADH-ferredoxinNAP reductase | - |
Pseudomonas putida |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.12.12 | 25 | - |
room temperature, ferredoxinNAP reductase, t1/2: 8 h | Pseudomonas sp. |
1.18.1.3 | 0.5 | - |
5 d, 30% loss of activity | Pseudomonas sp. |
1.18.1.3 | 21 | - |
room temperature, 8 h, 50% loss of activity | Pseudomonas sp. |
1.18.1.7 | - |
20 | the purified enzyme is unstable at room temperature. It loses 50% of its cytochrome c reductase activity within the first 8 h. At 0 to 5°C, the purified enzyme retains 70% of its cytochrome c reductase activity after 5 days | Pseudomonas putida |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.12.12 | additional information | - |
ferredoxin reductaseNAP, pI: 6.3 | Pseudomonas sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.12.12 | FAD | 1 mol FAD/mol enzyme in flavin-reconstituted protein | Pseudomonas sp. | |
1.14.12.12 | FAD | component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD | Pseudomonas sp. | |
1.14.12.12 | 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. | |
1.14.12.12 | 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. | |
1.14.12.12 | NADH | - |
Pseudomonas sp. | |
1.14.12.12 | NADPH | ferredoxinNAP reductase | Pseudomonas sp. | |
1.14.12.12 | NADPH | can replace NADH with 39% | Pseudomonas sp. | |
1.18.1.3 | FAD | 1 mol of FAD is bound per mol of enzyme | Pseudomonas sp. | |
1.18.1.3 | NADH | - |
Pseudomonas sp. | |
1.18.1.3 | NADPH | 39% of the activity with NADH in the reaction with cytochrome c | Pseudomonas sp. | |
1.18.1.7 | FAD | the enzyme binds 1 mol of FAD per mol of enzyme protein | Pseudomonas putida | |
1.18.1.7 | NADH | - |
Pseudomonas putida |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.18.1.7 | Pseudomonas putida | calculated from amino acid sequence | - |
6.3 |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
1.18.1.7 | 10 | - |
pH and temperature not specified in the publication | Pseudomonas putida | iodoacetate |