General Stability | Organism |
---|---|
10% ethanol and 10% glycerol are required for stability | Pseudomonas sp. |
DTT stabilizes | Pseudomonas sp. |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Pseudomonas sp. | 5737 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | component B, the terminal oxygenase ISPNAP is an iron-sulfur protein, oxidized ISPNAP binds naphthalene without conformational changes that affect its FeS-chromophores, ISPNAP contains 6 g-atom Fe2+ and 4 g-atom acid-labile sulfur per mol enzyme, the enzyme complex is not stimulated by exogenous Fe2+ | 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. |
20000 | - |
alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE | Pseudomonas sp. |
55000 | - |
alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE | Pseudomonas sp. |
158000 | - |
component B, i.e. oxygenase ISPNAP, gel filtration | Pseudomonas sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
naphthalene + NADH + O2 | Pseudomonas sp. | - |
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? | |
naphthalene + NADH + O2 | Pseudomonas sp. NCIB 9816 | - |
(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas sp. | - |
- |
- |
Pseudomonas sp. NCIB 9816 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
component B i.e. the terminal oxygenase ISPNAP, DEAE-Sephadex, DEAE-cellulose, octyl-Sepharose, presence of 10% ethanol and 10% glycerol is required to maintain stability | Pseudomonas sp. |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.37 | - |
in the presence of partially purified components A and C of the 3 component enzyme system plus FAD | Pseudomonas sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
naphthalene + NADH + O2 | - |
Pseudomonas sp. | cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? | |
naphthalene + NADH + O2 | - |
Pseudomonas sp. NCIB 9816 | cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? | |
naphthalene + NADH + O2 | - |
Pseudomonas sp. | (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? | |
naphthalene + NADH + O2 | - |
Pseudomonas sp. NCIB 9816 | (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | alpha2beta2 2 * 55000 + 2 * 20000, terminal oxygenase ISPNAP, SDS-PAGE | Pseudomonas sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pseudomonas sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD | Pseudomonas sp. | |
NADH | requirement, the oxygenase accepts two electrons from NADH, the reduction requires component A and C as mediators | Pseudomonas sp. |