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Literature summary extracted from
- Mixed function oxidation. V. Flavin interaction with a reduced diphosphopyridine nucleotide dehydrogenase, one of the enzymes participating in camphor lactonization (1966), J. Biol. Chem., 241, 1194-1205.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.108 | dichlorophenolindophenol | activation, enhances NADH-oxidation | Pseudomonas putida |  |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.108 | 2,2'-bipyridine | inhibition of the whole enzyme complex, but not of the components alone | Pseudomonas putida | |
| 1.14.14.108 | DTNB | mild inhibition, dehydrogenase | Pseudomonas putida | |
| 1.14.14.108 | H2O2 | mild inhibition, dehydrogenase | Pseudomonas putida | |
| 1.14.14.108 | KI | dehydrogenase | Pseudomonas putida | |
| 1.14.14.108 | methylene blue | dehydrogenase | Pseudomonas putida | |
| 1.14.14.108 | NEM | partial inhibition, dehydrogenase | Pseudomonas putida | |
| 1.14.14.108 | p-hydroxymercuribenzoate | incomplete inhibition, dehydrogenase, reversible by GSH or DTT | Pseudomonas putida | |
| 1.14.14.108 | sodium arsenite | mild inhibition, dehydrogenase | Pseudomonas putida | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.108 | 0.003 | - |
FMN | - |
Pseudomonas putida | |
| 1.14.14.108 | 0.019 | - |
FAD | - |
Pseudomonas putida | |
| 1.14.14.108 | 0.1 | - |
NADH | interaction with apoenzyme/FMN-complex | Pseudomonas putida | |
| 1.14.14.108 | 0.21 | - |
NADH | interation with apoenzyme/2FAD-complex | Pseudomonas putida | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.108 | cytoplasm | - |
Pseudomonas putida | 5737 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.108 | additional information | - |
multi-component enzyme, consisting of at least two components: a reductase E2 and an oxygenating component E1 | Pseudomonas putida |
| 1.14.14.108 | 36000 | - |
reductase component E2, low speed sedimentation without reaching equilibrium | Pseudomonas putida |
| 1.14.14.108 | 120000 | - |
- |
Pseudomonas putida |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.108 | Pseudomonas putida | - |
wild type strain C1B (PpG1) | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.108 | component E1, FMN-reductase | Pseudomonas putida |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.108 | 417 | - |
purified component E1 NADH-dehydrogenase | Pseudomonas putida |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.14.14.108 | -15°C, in 0.05 M Tris/HCl or potassium phosphate buffer, pH 7.2, the dehydrogenase is stable for months | Pseudomonas putida |
| 1.14.14.108 | 0°C, in buffer, the dehydrogenase is stable for a week, in very dilute solutions, the dehydrogenase is stable without protective agents | Pseudomonas putida |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.108 | (+)-5-oxo-1,2-campholide + FAD + H2O | - |
Pseudomonas putida | (+)-bornane-2,5-dione + FADH2 + O2 | - |
r | |
| 1.14.14.108 | (+)-bornane-2,5-dione + FMNH2 + O2 | i.e. 2,5-diketocamphane | Pseudomonas putida | 3,4,4-trimethyl-5-carboxy-methyl-DELTA2-cyclopentenone + FMN + H2O | i.e. cyclopentenoic acid | ? | |
| 1.14.14.108 | additional information | rubredoxin not mentioned | Pseudomonas putida | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.14.108 | More | multi-component enzyme, consisting of at least two components: a reductase E2 and an oxygenating component E1 | Pseudomonas putida |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.108 | 25 | - |
assay at | Pseudomonas putida |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.108 | additional information | - |
additional information | - |
Pseudomonas putida | |
| 1.14.14.108 | 317 | - |
NADH | - |
Pseudomonas putida | |
| 1.14.14.108 | 650 | - |
FAD | component E2 | Pseudomonas putida | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.108 | 5 | - |
NADH-dehydrogenase | Pseudomonas putida |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.108 | 7 | 8 | 70% of activity maximum at pH 7 and pH 8, NADH-dehydrogenase | Pseudomonas putida |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.108 | FAD | 2 mol will bind reversibly at the binding site of the apoprotein of the dehydrogenase, in the presence of FMN only 1 mol | Pseudomonas putida | |
| 1.14.14.108 | FMN | - |
Pseudomonas putida | |
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