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Information on EC 1.6.3.3 - NADH oxidase (H2O2-forming)
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1.6.3.3 NADH oxidase (H2O2-forming)IUBMB Comments
A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4, NADH oxidase (H2O-forming)) . The enzymes from the anaerobic archaea Methanocaldococcus jannaschii and Pyrococcus furiosus also produce low amounts of H2O. Unlike EC 1.6.3.1 (NAD(P)H oxidase) it has no activity towards NADPH.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
nox-1, noxb-1, noxa-1, noxa2, mj0649, mjnox, h2o2-forming nadh oxidase, af0395, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H2O2-forming NADH oxidase
NADH:O2 oxidoreductase
NOX
Nox-1
PH0311
PhNOX
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + O2 = NAD+ + H2O2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
NADH:oxygen oxidoreductase (H2O2-forming)
A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4, NADH oxidase (H2O-forming)) [1]. The enzymes from the anaerobic archaea Methanocaldococcus jannaschii [6] and Pyrococcus furiosus [3] also produce low amounts of H2O. Unlike EC 1.6.3.1 (NAD(P)H oxidase) it has no activity towards NADPH.
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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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
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 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
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
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
divalent cations are not required for activity
additional information
divalent cations are not required for activity
additional information
-
divalent cations are not required for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis-(2-nitrobenzoate)
-
1 mM, 7 min, 50% loss of activity
dithiothreitol
2 mM, rapid decrease in activity to less than 10% of the activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
n-dodecyl beta-D-maltoside
0.5%, increases activity about twofold
FAD
flavoprotein, addition of 0.06 mM results in 3.7fold stimulation
FAD
flavoprotein, Addition of 0.06 mM results in about 2.5fold stimulation
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression.
Carcinoma
XPC silencing in normal human keratinocytes triggers metabolic alterations through NOX-1 activation-mediated reactive oxygen species.
Carcinoma in Situ
A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression.
Carcinoma, Squamous Cell
XPC silencing in normal human keratinocytes triggers metabolic alterations through NOX-1 activation-mediated reactive oxygen species.
Colonic Neoplasms
TLR-4 signalling accelerates colon cancer cell adhesion via NF-?B mediated transcriptional up-regulation of Nox-1.
COVID-19
Severe COVID-19 Is Characterized by an Impaired Type I Interferon Response and Elevated Levels of Arginase Producing Granulocytic Myeloid Derived Suppressor Cells.
COVID-19
Transcriptome and Functions of Granulocytic Myeloid-Derived Suppressor Cells Determine their Association with Disease Severity of COVID-19.
Dental Caries
Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein.
Galactosemias
Impaired NADPH oxidase activity in peripheral blood lymphocytes of galactosemia patients.
Heart Failure
Exendin-4 therapy still offered an additional benefit on reducing transverse aortic constriction-induced cardiac hypertrophy-caused myocardial damage in DPP-4 deficient rats.
Hypertension
A possible correlation between the correction of endothelial dysfunction and normalization of high blood pressure levels by 1,3,4-oxadiazole derivative, an L-type Ca2+ channel blocker in deoxycorticosterone acetate and N(G)-nitro-l-arginine hypertensive rats.
Infertility, Female
NADPH oxidases NOX-1 and NOX-2 require the regulatory subunit NOR-1 to control cell differentiation and growth in Neurospora crassa.
Myocardial Infarction
Left ventricular remodeling after myocardial infarction in mice with targeted deletion of the NADPH oxidase subunit gp91(PHOX).
Neoplasms
Chronic peroxisome proliferator-activated receptor?/? agonist GW0742 prevents hypertension, vascular inflammatory and oxidative status, and endothelial dysfunction in diet-induced obesity.
Neoplasms
FK228 and oncogenic H-Ras synergistically induce Mek1/2 and Nox-1 to generate reactive oxygen species for differential cell death.
Neoplasms
Intervention of human breast cell carcinogenesis chronically induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine.
Neoplasms
Protective vascular effects of quercitrin in acute TNBS-colitis in rats: the role of nitric oxide.
Neoplasms
Punicalagin and (-)-Epigallocatechin-3-Gallate Rescue Cell Viability and Attenuate Inflammatory Responses of Human Epidermal Keratinocytes Exposed to Airborne Particulate Matter PM10.
Neoplasms
Reactive oxygen species-linked regulation of the multidrug resistance transporter P-glycoprotein in Nox-1 overexpressing prostate tumor spheroids.
Neuralgia
Thymus algeriensis and Thymus fontanesii exert neuroprotective effect against chronic constriction injury-induced neuropathic pain in rats.
Obesity
Effect of obesity reduction on preservation of heart function and attenuation of left ventricular remodeling, oxidative stress and inflammation in obese mice.
Obesity
Protein Disulphide Isomerase and NADPH Oxidase 1 Cooperate to Control Platelet Function and Are Associated with Cardiometabolic Disease Risk Factors.
Sepsis
Rapid NOS-1-derived nitric oxide and peroxynitrite formation act as signaling agents for inducible NOS-2 expression in vascular smooth muscle cells.
Sepsis
Vascular Dysfunction in Sepsis: Effects of the Peroxynitrite Decomposition Catalyst MnTMPyP.
Shock, Septic
Rapid NOS-1-derived nitric oxide and peroxynitrite formation act as signaling agents for inducible NOS-2 expression in vascular smooth muscle cells.
Skin Neoplasms
XPC silencing in normal human keratinocytes triggers metabolic alterations through NOX-1 activation-mediated reactive oxygen species.
Stomach Ulcer
The implication of the crosstalk of Nrf2 with NOXs, and HMGB1 in ethanol-induced gastric ulcer: Potential protective effect is afforded by Raspberry Ketone.
Urinary Bladder Neoplasms
Differential induction of reactive oxygen species through Erk1/2 and Nox-1 by FK228 for selective apoptosis of oncogenic H-Ras-expressing human urinary bladder cancer J82 cells.
Urinary Bladder Neoplasms
Oncogenic H-Ras, FK228, and exogenous H2O2 cooperatively activated the ERK pathway in selective induction of human urinary bladder cancer J82 cell death.
Vascular Calcification
The Role of AGE/RAGE Signaling in Diabetes-Mediated Vascular Calcification.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0037
beta-NADH
pH and temperature not specified in the publication
additional information
additional information
-
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
115
beta-NADH
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4 - 8.4
pH 4.4: about 70% of maximal activity, pH 8.4: about 90% of maximal activity
4.5 - 8
pH 4.5: about 90% of maximal activity, pH 8.0: about 50% of maximal activity
5 - 8
pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
5.5 - 8.5
-
pH 5.5: 73% of maximal activity (50 mM Mes buffer), pH 8.5: 81% of maximal activity (50 mM Mops buffer)
6 - 9.5
pH 6.0: about 60% of maximal activity, pH 9.5: about 60% of maximal activity
6.5 - 9
pH 6.5: about 55% of maximal activity, pH 9.0: about 55% of maximal activity
7.9 - 11
-
pH 7.8: about 60% of maximal activity, pH 11.0: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 58
-
the activity increases with the temperature, as tested from 30°C to 58°C
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 90
active from room temperature to 90°C. At 50°C, the activity of the recombinant enzyme is half that at 80°C
30 - 50
30°C; about 75% of maximal activity, 50°C: about 80% of maximal activity
55 - 100
55°C: about 60% of maximal activity, 100°C: about 80% of maximal activity
60 - 90
60°C: about 50% of maximal activity, 90°C: about 95% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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