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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+ +

O2
= 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

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.3 With oxygen as acceptor
                1.6.3.4 NADH oxidase (H2O-forming)

Engineering

Engineering on EC 1.6.3.4 - NADH oxidase (H2O-forming)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C42A
-
produces H2O2, 90% loss of NADH oxidase activity
D170R
-
18.8% loss of activity
D219R
-
37.6% loss of activity
D247R
-
60.4% loss of activity
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
D359R
-
91% loss of activity
E316R
-
91% loss of activity
C42A
-
produces H2O2, 90% loss of NADH oxidase activity
-
C44A
-
80% of wild-type activity, production of H2O2 rather than H2O
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
K126R
-
the mutation reduces NADH oxidase activity to about 85%
K161R
-
the mutation reduces NADH oxidase activity to about 85%
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
K241R
-
the mutant shows wild type activity
K265R
-
the mutant shows wild type activity
K278R
-
the mutant shows wild type activity
K374R
-
the mutation reduces NADH oxidase activity to about 50%
K393R
-
the mutation reduces NADH oxidase activity to about 70%