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
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1.6.3.3 NADH oxidase (H2O2-forming)Advanced search results
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Substrates Products on EC 1.6.3.3 - NADH oxidase (H2O2-forming)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 NADH + H+ + O2
2 NAD+ + 2 H2O
the enzyme produces both H2O and H2O2. 62% of NADH-derived reducing equivalents are recovered as H2O2 and the rest probably generates H2O. The NADPH oxidase activity is about 5% compared to the activity with NADH
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
the enzyme produces both H2O and H2O2, It is highly specific for NADH, little or no activity with NADPH. NOX1 produces 23% water and 77% H2O2 as products under the assay conditions given
-
-
?
NADPH + H+ + O2
NAD+ + H2O2
the enzyme produces both H2O and H2O2. 62% of NADH-derived reducing equivalents are recovered as H2O2 and the rest probably generates H2O. The NADPH oxidase activity is about 5% compared to the activity with NADH
-
-
?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
the enzyme is specific for beta-NADH. No activity with alpha-NADH, alpha-NADPH, or beta-NADPH
-
-
?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
the enzyme is specific for beta-NADH. No activity with alpha-NADH, alpha-NADPH, or beta-NADPH
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme also acts as an NADH:ferredoxin oxidoreductase
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme also acts as an NADH:ferredoxin oxidoreductase
-
-
?
NADH + H+ + O2
NAD+ + H2O2
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration
-
-
?
NADH + H+ + O2
NAD+ + H2O2
the enzyme predominantly produces H2O2. No activity with NADPH. The enzyme also shows activity with 2,6-dichloroindophenol, ferricyanide, menadione, and 2,3-dimethyl-1,4-naphthoquinone
-
-
?
NADH + H+ + O2
NAD+ + H2O2
the enzyme predominantly produces H2O2. No activity with NADPH. The enzyme also shows activity with 2,6-dichloroindophenol, ferricyanide, menadione, and 2,3-dimethyl-1,4-naphthoquinone. Very low activity with cytochrome c
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme is highly specific for NADH. No formation of H2O
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme is highly specific for NADH. No formation of H2O
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme produces both H2O and H2O2, It is highly specific for NADH, little or no activity with NADPH. NOX1 produces 23% water and 77% H2O2 as products under the assay conditions given
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
oxidizes specifically beta-NADH in the presence of molecular oxygen
-
-
?
NADH + H+ + O2
NAD+ + H2O2
Nox-1 is a protective protein against oxygen toxicity
-
-
?
NADH + H+ + O2
NAD+ + H2O2
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
-
-
?
NADH + H+ + O2
NAD+ + H2O2
the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
NADH + H+ + O2
NAD+ + H2O2
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
-
-
?
NADH + H+ + O2
NAD+ + H2O2
the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
oxidizes specifically beta-NADH in the presence of molecular oxygen
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
an oxygen-removing system present in Thermotoga maritima is proposed to work in two steps: firstly by converting O2 to hydrogen peroxide by the NADH oxidase, and secondly by reducing the hydrogen peroxide to water by an NADH peroxidase or rubrerythrin or alkyl hydroperoxide reductase
-
-
?
NADH + H+ + O2
NAD+ + H2O2
-
the enzyme is highly specific for NADH, no activity with NADPH. Highest activity using O2 as an electron acceptor. Compared to lower activities for benzyl viologen (20%) and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB, 7%), while no activity is observed when FAD, FMN, or riboflavin is used as the electron acceptor
-
-
?
additional information
?
-
the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c
-
-
?
additional information
?
-
-
the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c
-
-
?
