1.6.3.3: NADH oxidase (H2O2-forming)
This is an abbreviated version!
For detailed information about NADH oxidase (H2O2-forming), go to the full flat file.
Reaction
Synonyms
AF0395, H2O2-forming NADH oxidase, H2O2-forming reduced nicotinamide adenine dinucleotide oxidase, MJ0649, MJNox, NADH:O2 oxidoreductase, NOX, Nox-1, NOX1, NoxA-1, NoxA2, NoxB-1, PH0311, PhNOX
ECTree
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Cofactor
Cofactor on EC 1.6.3.3 - NADH oxidase (H2O2-forming)
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FAD
-
a flavoprotein, contains 1.8 mol of non-covalently bound FAD per mol of native enzyme
FAD
-
flavoprotein. FAD remains enzyme-bound at room temperature. At least 82% of the FAD remains in the enzyme-bound form at 75°C. FMN is not able to substitute for FAD in the substrate-level FAD-dependent portion of the reaction. The Km-value for O2 is above 0.11 mM
FAD
-
flavoprotein. The enzyme contains 1.9 mol of FAD per mol native enzyme
FAD
required for activity. 1.1 mol of FAD per mol of enzyme. The FAD cofactor is associated noncovalently with the protein
FAD
-
requires the presence of a flavin cofactor, showing a high specificity for FAD. The enzyme does not contain a flavin molecule
FAD
-
requires the presence of a flavin cofactor, showing a high specificity for FAD. The enzyme is purified as an FAD-containing protein
FAD
-
the enzyme is FAD dependent. The activity is 5fold stimulated if the reaction assay contains FAD (0.05 mM). At FAD concentrations above 50 mM the enzyme activity is essentially exogenous flavin independent
NADH
-
the enzyme is highly specific for NADH, little or no activity with NADPH
NADH
the enzyme is highly specific for NADH, no activity with NADPH
NADH
-
the enzyme is highly specific for NADH, relative activity with NADPH is 2% compared to the activity with NADH
NADH
the NADPH oxidase activity is about 5% compared to the activity with NADH