Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermococcus profundus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
2 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE | Thermococcus profundus |
50000 | - |
6 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE | Thermococcus profundus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 NADH + H+ + O2 | Thermococcus profundus | 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 | NAD+ + 2 H2O | - |
? | |
2 NADPH + 2 H+ + O2 | Thermococcus profundus | 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 | 2 NADP+ + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus profundus | B2G3S1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
2 NADPH + 2 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 | 2 NADP+ + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE | Thermococcus profundus |
hexamer | 6 * 50000, the enzyme exists as a dimeric form under normal/anaerobic conditions, and the dimers assemble into hexamers under stress. H2O2 is the strongest stressor, followed by O2 and cold stress, SDS-PAGE | Thermococcus profundus |
Synonyms | Comment | Organism |
---|---|---|
NOXtp | - |
Thermococcus profundus |
General Information | Comment | Organism |
---|---|---|
physiological function | NAD(P)H oxidase 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 |