EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.6.3.2 | 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 |
- |
? |
| 1.6.3.2 | 2 NADH + H+ + O2 |
reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability |
Thermococcus profundus |
NAD+ + 2 H2O |
- |
? |
| 1.6.3.2 | 2 NADH + H+ + O2 |
NADPH is more efficient as electron donor compared to NADH |
Giardia intestinalis |
NAD+ + 2 H2O |
- |
? |
| 1.6.3.2 | 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 |
- |
? |
| 1.6.3.2 | 2 NADH + H+ + O2 |
reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2). Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability |
Thermococcus profundus |
NAD+ + 2 H2O |
- |
? |
| 1.6.3.2 | 2 NADH + H+ + O2 |
NADPH is more efficient as electron donor compared to NADH |
Giardia intestinalis BRIS/83/HEPU/106 |
NAD+ + 2 H2O |
- |
? |
| 1.6.3.2 | 2 NADPH + 2 H+ + O2 |
- |
Giardia intestinalis |
2 NADP+ + 2 H2O |
- |
? |
| 1.6.3.2 | 2 NADPH + 2 H+ + O2 |
reaction is catalyzed by the native dimeric protein under physiological conditions (low amounts of O2) to detoxify O2. Oxidative stress induced conformational change implicates a functional switch of the enzyme. The oxidized enzyme protein can accelerate the aggregation of partially unfolded proteins. It can also bind nucleic acids and produce H2O2 to destroy DNA and RNA with the ultimate function of decreasing cell viability |
Thermococcus profundus |
2 NADP+ + 2 H2O |
- |
? |
| 1.6.3.2 | 2 NADPH + 2 H+ + O2 |
the enzyme may be involved in maintenance of an optimum intracellular redox ratio |
Giardia intestinalis |
2 NADP+ + 2 H2O |
- |
? |
| 1.6.3.2 | 2 NADPH + 2 H+ + O2 |
O2 is the most effective electron acceptor, NADH or NADPH are not oxidized anaerobically |
Giardia intestinalis |
2 NADP+ + 2 H2O |
- |
? |
