Application | Comment | Organism |
---|---|---|
synthesis | the isolated enzyme is used for the synthesis of 2,5-dihydroxypyridine, a precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy | Pseudomonas fluorescens |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Pseudomonas fluorescens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5,5'-dithiobis(2-nitrobenzoate) | 1 mM, complete inhibition | Pseudomonas fluorescens | |
Ag2SO4 | 1 mM, complete inhibition | Pseudomonas fluorescens | |
CuCl2 | 1 mM, complete inhibition | Pseudomonas fluorescens | |
HgCl2 | 1 mM, complete inhibition | Pseudomonas fluorescens | |
additional information | no significant effect on enzyme activity is found with metal-chelating agents such o-phenanthroline, 8-hydroxyquinoline, EDTA, disodium 4,5-dihydroxy-m-benzenedisulfonate, fluoride and azide, and other compounds such as KCl, LiCl, NaCl, BaCl2, CaCl2, MnCl2, MgCl2, PbCl2, ZnCl2, CoCl2, SnCl2, FeSO4, FeCl3, NiCl2, CdCl2, AlCl3, iodoacetic acid, hydroxylamine, phenylhydrazine, semicarbazide, cysteamine, alpha,alpha'-dipyridyl and urea | Pseudomonas fluorescens | |
N-ethylmaleimide | 1 mM, 69% inhibition | Pseudomonas fluorescens | |
nicotinate | potent competitive inhibitor | Pseudomonas fluorescens | |
p-chloromercuribenzoate | 1 mM, complete inhibition | Pseudomonas fluorescens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.098 | - |
6-Hydroxynicotinate | pH 7.0, 30°C | Pseudomonas fluorescens | |
0.15 | - |
4-hydroxybenzoate | pH 7.0, 30°C | Pseudomonas fluorescens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound to | Pseudomonas fluorescens | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
42886 | - |
1 * 42886, including the starting methionine, calculated from sequence | Pseudomonas fluorescens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-hydroxynicotinate + NADH + H+ + O2 | Pseudomonas fluorescens | aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH | 2,5-dihydroxypyridine + NAD+ + H2O + CO2 | - |
? | |
6-hydroxynicotinate + NADH + H+ + O2 | Pseudomonas fluorescens TN5 | aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH | 2,5-dihydroxypyridine + NAD+ + H2O + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas fluorescens | - |
- |
- |
Pseudomonas fluorescens TN5 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Pseudomonas fluorescens |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
6.67 | - |
- |
Pseudomonas fluorescens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxybenzoate + NADH + H+ + O2 | 6.0% relative activity compared with 6-hydroxynicotinate | Pseudomonas fluorescens | hydroquinone + NAD+ + H2O + CO2 | - |
? | |
4-hydroxybenzoate + NADH + H+ + O2 | 6.0% relative activity compared with 6-hydroxynicotinate | Pseudomonas fluorescens TN5 | hydroquinone + NAD+ + H2O + CO2 | - |
? | |
6-hydroxynicotinate + NADH + H+ + O2 | aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH | Pseudomonas fluorescens | 2,5-dihydroxypyridine + NAD+ + H2O + CO2 | - |
? | |
6-hydroxynicotinate + NADH + H+ + O2 | NADH is 5times more effective than NADPH | Pseudomonas fluorescens | 2,5-dihydroxypyridine + NAD+ + H2O + CO2 | - |
? | |
6-hydroxynicotinate + NADH + H+ + O2 | aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH | Pseudomonas fluorescens TN5 | 2,5-dihydroxypyridine + NAD+ + H2O + CO2 | - |
? | |
6-hydroxynicotinate + NADH + H+ + O2 | NADH is 5times more effective than NADPH | Pseudomonas fluorescens TN5 | 2,5-dihydroxypyridine + NAD+ + H2O + CO2 | - |
? | |
additional information | 3-hydroxybenzoate (0.49% relative activity compared with 6-hydroxynicotinate), 2-hydroxybenzoate (0.18% compared with 6-hydroxynicotinate), 2-hydroxynicotinate (0.31% relative activity compared with 6-hydroxynicotinate) and 6-hydroxypyrazine carboxylate (0.19% relative activity compared with 6-hydroxynicotinate) are less effecive substrates or, in the case of nicotinate, 6-methylnicotinate and benzoate, not substrates at all | Pseudomonas fluorescens | ? | - |
? | |
additional information | 3-hydroxybenzoate (0.49% relative activity compared with 6-hydroxynicotinate), 2-hydroxybenzoate (0.18% compared with 6-hydroxynicotinate), 2-hydroxynicotinate (0.31% relative activity compared with 6-hydroxynicotinate) and 6-hydroxypyrazine carboxylate (0.19% relative activity compared with 6-hydroxynicotinate) are less effecive substrates or, in the case of nicotinate, 6-methylnicotinate and benzoate, not substrates at all | Pseudomonas fluorescens TN5 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 40000-42000, SDS-PAGE | Pseudomonas fluorescens |
monomer | 1 * 42886, including the starting methionine, calculated from sequence | Pseudomonas fluorescens |
Synonyms | Comment | Organism |
---|---|---|
6-hydroxynicotinic acid 3-monooxygenase | - |
Pseudomonas fluorescens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
- |
Pseudomonas fluorescens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
pH 7.0, 10 min, in the absence of FAD, apoenzyme is stable below | Pseudomonas fluorescens |
40 | - |
pH 7.0, 10 min, in the presence of 0.5 mM FAD, holoenzyme is stable below | Pseudomonas fluorescens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
- |
Pseudomonas fluorescens |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | 35°C, 10 min, stable between pH 6.0 and pH 9.0 | Pseudomonas fluorescens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the enzyme activity is NADH-dependent and FAD-dependent. The holoenzyme contains 1 M of FAD per 1 M of enzyme. FAD gradually dissociates from the enzyme during purification. Without FAD, no pure enzyme activity is observed, but after the addition of FAD, the apoenzyme is activated immediately | Pseudomonas fluorescens | |
additional information | riboflavin or FMN do not serve as enzyme cofactors | Pseudomonas fluorescens | |
NADH | the enzyme activity is NADH-dependent and FAD-dependent. NADH is 5times more effective than NADPH | Pseudomonas fluorescens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.49 | - |
nicotinate | - |
Pseudomonas fluorescens |