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Literature summary for 1.6.3.2 extracted from
- TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus kodakaraensis exhibiting higher enzymatic activity with NADPH (2013), J. Biosci. Bioeng., 116, 39-44.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Thermococcus kodakarensis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.24 | - |
NADH | pH 7.8, 75°C | Thermococcus kodakarensis |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 48610 | - |
6 * 48610, sequence calculation | Thermococcus kodakarensis |
| 49375 | - |
6 * 49375, mass spectrometry | Thermococcus kodakarensis |
| 300000 | - |
gel filtration | Thermococcus kodakarensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | Q5JGP4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermococcus kodakarensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3 NADH + 3 H+ + 2 O2 | approximately 75% H2O and 25% H2O is produced. Km value of the enzyme towards NADH and NADPH is almost the same whereas specific activity is higher with NADPH compared to NADH | Thermococcus kodakarensis | 3 NAD+ + H2O | - |
? | |
| 3 NADPH + 3 H+ + 2 O2 | approximately 87% H2O and 13% H2O2 is produced. Km value of the enzyme towards NADH and NADPH is almost the same whereas specific activity is higher with NADPH compared to NADH | Thermococcus kodakarensis | 3 NADP+ + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 48610, sequence calculation | Thermococcus kodakarensis |
| hexamer | 6 * 49375, mass spectrometry | Thermococcus kodakarensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| KOD1 | - |
Thermococcus kodakarensis |
| NAD(P)H oxidase | - |
Thermococcus kodakarensis |
| TK1299 | - |
Thermococcus kodakarensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
- |
Thermococcus kodakarensis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | 80 | 70°C: about 60% of maximal activity, 80°C: about 70% of maximal activity | Thermococcus kodakarensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 100 | - |
150 min, less than 5% loss of activity | Thermococcus kodakarensis |
| 120 | - |
secondary structure of the enzyme is not stable at this temperature | Thermococcus kodakarensis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 68 | - |
NADH | pH 7.8, 75°C | Thermococcus kodakarensis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Thermococcus kodakarensis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8.5 | pH 7.5: about 70% of maximal activity, pH 8.5: about 70% of maximal activity | Thermococcus kodakarensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | tightly bound, 0.5 FAD attached per subunit | Thermococcus kodakarensis | |
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