Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermococcus profundus |
Protein Variants | Comment | Organism |
---|---|---|
C122A | mutant contains tightly bound FAD. Mutant has similar NADH and NADPH oxidase activity to that of the wild-type protein | Thermococcus profundus |
C45A | mutant contains tightly bound FAD. Mutant has less than 10% of the NAD(P)H oxidase activity of the wild-type protein. Mutation alters the reaction to produce H2O2 instead of H2O | Thermococcus profundus |
C45A/C122A | mutant contains tightly bound FAD. Mutant has less than 10% of the NAD(P)H oxidase activity of the wild-type protein. Mutation alters the reaction to produce H2O2 instead of H2O | Thermococcus profundus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.012 | - |
NADPH | pH 7.2, 75°C | Thermococcus profundus | |
0.053 | - |
NADH | pH 7.2, 75°C | Thermococcus profundus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
49000 | - |
6 * 49000, ring-shaped hexameric form, SDS-PAGE | Thermococcus profundus |
300000 | - |
gel filtration | Thermococcus profundus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 NAD(P)H + H+ + O2 | Thermococcus profundus | in anaerobes, flavin-dependent NAD(P)H oxidases play an important role protecting organisms from oxidative stress | NAD(P)+ + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus profundus | B2G3S1 | - |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes | Thermococcus profundus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 NAD(P)H + H+ + O2 | in anaerobes, flavin-dependent NAD(P)H oxidases play an important role protecting organisms from oxidative stress | Thermococcus profundus | NAD(P)+ + 2 H2O | - |
? | |
2 NADH + H+ + O2 | predominantly converts O2 to H2O, but not to H2O2. When NADPH oxidation is performed at 80°C, approximately 2% of the NADPH supplied is used to produce H2O2. Cys45 participates in the direct four-electron reduction of O2 to H2O, and the Cys45 mutation alters the reaction to produce H2O2 instead of H2O. NADPH is more efficient as electron donor compared to NADH | Thermococcus profundus | NAD+ + 2 H2O | - |
? | |
2 NADPH + 2 H+ + O2 | predominantly converts O2 to H2O. When NADPH oxidation is performed at 80°C, approximately 7% of the NADPH supplied is used to produce H2O2. Cys45 participates in the direct four-electron reduction of O2 to H2O, and the Cys45 mutation alters the reaction to produce H2O2 instead of H2O. NADPH is more efficient as electron donor compared to NADH | Thermococcus profundus | 2 NADP+ + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | 6 * 49000, ring-shaped hexameric form, SDS-PAGE | Thermococcus profundus |
Synonyms | Comment | Organism |
---|---|---|
NOXtp | - |
Thermococcus profundus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
- |
Thermococcus profundus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 70 | 50°C: about 40% of maximal activity, 70°C: about 70% of maximal activity | Thermococcus profundus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.5 | - |
NADPH | pH 7.2, 75°C | Thermococcus profundus | |
6.2 | - |
NADH | pH 7.2, 75°C | Thermococcus profundus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 8 | - |
Thermococcus profundus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 8.5 | pH 6.5: about 70% of maximal activity, pH 8.5: about 45% of maximal activity | Thermococcus profundus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | contains 0.7-0.9 mol FAD per subunit | Thermococcus profundus | |
NADH | NADPH is more efficient as electron donor compared to NADH | Thermococcus profundus | |
NADPH | NADPH is more efficient as electron donor compared to NADH | Thermococcus profundus |
General Information | Comment | Organism |
---|---|---|
physiological function | in anaerobes, flavin-dependent NAD(P)H oxidases play an important role protecting organisms from oxidative stress | Thermococcus profundus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
116.9 | - |
NADH | pH 7.2, 75°C | Thermococcus profundus | |
206.6 | - |
NADPH | pH 7.2, 75°C | Thermococcus profundus |