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Literature summary for 1.14.13.163 extracted from
- Mechanism of the 6-hydroxy-3-succinoyl-pyridine 3-monooxygenase flavoprotein from Pseudomonas putida S16 (2014), J. Biol. Chem., 289, 29158-29170 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene hspB, phylogenetic analysis and tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Pseudomonas putida |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | stopped-flow spectroscopy and kinetic analysis | Pseudomonas putida | |
| 0.173 | - |
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate | pH 8.0, 25°C, recombinant His-tagged enzyme | Pseudomonas putida |  |
| 0.0294 | - |
NADH | pH 8.0, 25°C, recombinant His-tagged enzyme | Pseudomonas putida | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 | Pseudomonas putida | - |
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O | - |
? | |
| 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 | Pseudomonas putida S16 | - |
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | - |
- |
- |
| Pseudomonas putida S16 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Pseudomonas putida |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -80°C, purified recombinant His-tagged enzyme HspB, as a frozen solution or dry powder, no change in activity for at least 3 months, pH 8.0 | Pseudomonas putida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | mass spectrometric analysis of substrates and products, with recombinant enzyme | Pseudomonas putida | ? | - |
? | |
| additional information | mass spectrometric analysis of substrates and products, with recombinant enzyme | Pseudomonas putida S16 | ? | - |
? | |
| 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 | - |
Pseudomonas putida | 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O | - |
? | |
| 4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 | - |
Pseudomonas putida S16 | 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| hspB | - |
Pseudomonas putida |
| 6-hydroxy-3-succinoyl-pyridine 3-monooxygenase | - |
Pseudomonas putida |
| HSP 3-monooxygenase | - |
Pseudomonas putida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Pseudomonas putida |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5.49 | - |
NADH | pH 8.0, 25°C, recombinant His-tagged enzyme | Pseudomonas putida | |
| 7.74 | - |
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate | pH 8.0, 25°C, recombinant His-tagged enzyme | Pseudomonas putida | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Pseudomonas putida |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Pseudomonas putida | |
| FAD | - |
Pseudomonas putida | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | 6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine | Pseudomonas putida |
| evolution | phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB | Pseudomonas putida |
| additional information | free H2O2 does not catalyze the HspB enzyme reaction | Pseudomonas putida |
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