1.6.3.4: NADH oxidase (H2O-forming)
This is an abbreviated version!
For detailed information about NADH oxidase (H2O-forming), go to the full flat file.
Reaction
2 NADH + 2 H+ + = 2 NAD+ + 2 H2O
Synonyms
H2O-forming NADH oxidase, LrNox, NADH oxidase, nicotinamide adenine dinucleotide oxidase, NOX, Nox-2, NoxA, NoxE, SpNox, water-forming NADH oxidase, YODC
ECTree
Advanced search results
Engineering
Engineering on EC 1.6.3.4 - NADH oxidase (H2O-forming)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
D251R
-
mutation improves the activity to 112%, 111%, and 244% of the wild-type at pH 6.5, pH 7.0, and pH 7.5, respectively. NADH has access to the substrate-binding site with a larger substrate loop due to the enhanced electrostatic repulsion between Arg251 and Arg243. In the D251R-NADH complex, the carboxyl of NADH additionally forms two hydrogen bonds with G154 due to the changed interaction of substrate and the residues in the catalytic sites, and the hydrogen bond with the oxygen of carbonyl in P295 is shortened from 2.9 to 2.0 A
D292A
-
mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity
G13A
-
mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity
G169A
-
loses nearly 100% of its activity, indicating that G169 is important for NADH binding
K182R
-
the mutation slightly enhances NADH oxidase activity by approximately 10%
K184A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184D
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184F
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184G
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184Q
-
the mutant shows reduced activity compared to the wild type enzyme
K184R
-
the mutation enhances NADH oxidase activity by approximately 50% and improves thermostability with 46.6 % longer half-life at 30°C