A flavoprotein (FAD). NADPH is a better substrate than NADH [1,3]. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea
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SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:oxygen oxidoreductase (H2O-forming)
A flavoprotein (FAD). NADPH is a better substrate than NADH [1,3]. By removal of oxygen the enzyme is involved in aerobic tolerance in the thermophilic anaerobic archaeon Thermococcus profundus and in Giardia intestinalis, a microaerophilic single-celled parasite of the order Diplomonadida.
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
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
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
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
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
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
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
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
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
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(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
overexpression of this enzyme in Giardia results in significantly enhanced growth under aerobic conditions. NADH oxidase could be thus an instrumental enzyme for the organism to adapt to and to tolerate an aerobic living environment
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
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
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
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
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
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