1.6.3.3: NADH oxidase (H2O2-forming)

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For detailed information about NADH oxidase (H2O2-forming), go to the full flat file.

Word Map on EC 1.6.3.3

1.6.3.3

apocynin

oxidase-1

p47phox

gp91phox

h2o-forming

synthesis

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

1 Oxidoreductases

1.6 Acting on NADH or NADPH

1.6.3 With oxygen as acceptor

1.6.3.3 NADH oxidase (H2O2-forming)

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Results	in table
12	Activating Compound
24	AA Sequence
4	Application
7	Cloned(Commentary)
21	Cofactor
4	Expression
7	General Information
43	Inhibitors
15	KM Value [mM]
2	Localization
5	Metals/Ions
28	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
25	Organism
1	Oxidation Stability
2	Pathway
14	pH Optimum
9	pH Range
2	pH Stability
1	pI Value
13	Purification (Commentary)
1	Reaction
20	Reference
2	Source Tissue
8	Specific Activity [micromol/min/mg]
2	Storage Stability
33	Substrates and Products (Substrate)
22	Subunits
25	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
5	Temperature Range [°C]
15	Temperature Stability [°C]
1	Turnover Number [1/s]

KM Value

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KM Value on EC 1.6.3.3 - NADH oxidase (H2O2-forming)

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0.0037

beta-NADH

Pyrococcus horikoshii

O58049

pH and temperature not specified in the publication

721957

0.00153 - 0.13

NADH

8 entries

0.043 - 2.9

5 entries

additional information

Pyrococcus furiosus

Km for NADH is below 4 mM, whereas the substrate-level FAD-dependent portion of the activity shows a Km for FAD of 0.044 mM. kcat for the oxidase reaction in the absence of substrate-level FAD is 4.8/s, while kcat for the reaction in the presence of substrate-level FAD is 11.1/s

722175