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EC Tree
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.
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,
more
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H2O2-forming NADH oxidase
H2O2-forming reduced nicotinamide adenine dinucleotide oxidase
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H2O2-forming NADH oxidase
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H2O2-forming NADH oxidase
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H2O2-forming NADH oxidase
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H2O2-forming NADH oxidase
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NADH:O2 oxidoreductase
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NADH:O2 oxidoreductase
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NOX
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Nox-1
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PH0311
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PhNOX
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NADH + H+ + O2 = NAD+ + H2O2
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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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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
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-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
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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
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?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
NADH + H+ + O2
NAD+ + H2O2
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
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?
additional information
?
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beta-NADH + H+ + O2
beta-NAD+ + H2O2
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-
-
?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
the enzyme is specific for beta-NADH. No activity with alpha-NADH, alpha-NADPH, or beta-NADPH
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-
?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
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-
-
?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
the enzyme is specific for beta-NADH. No activity with alpha-NADH, alpha-NADPH, or beta-NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme also acts as an NADH:ferredoxin oxidoreductase
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?
NADH + H+ + O2
NAD+ + H2O2
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme also acts as an NADH:ferredoxin oxidoreductase
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?
NADH + H+ + O2
NAD+ + H2O2
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration
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?
NADH + H+ + O2
NAD+ + H2O2
no activity with beta-NADPH
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?
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
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?
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
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme is highly specific for NADH, no activity with NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme is highly specific for NADH, no activity with NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme is highly specific for NADH. No formation of H2O
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme is highly specific for NADH. No formation of H2O
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?
NADH + H+ + O2
NAD+ + H2O2
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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
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?
NADH + H+ + O2
NAD+ + H2O2
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?
NADH + H+ + O2
NAD+ + H2O2
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oxidizes specifically beta-NADH in the presence of molecular oxygen
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?
NADH + H+ + O2
NAD+ + H2O2
Nox-1 is a protective protein against oxygen toxicity
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?
NADH + H+ + O2
NAD+ + H2O2
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
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?
NADH + H+ + O2
NAD+ + H2O2
the enzyme is highly specific for NADH, no activity with NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
absolute specificity for NADH
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?
NADH + H+ + O2
NAD+ + H2O2
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
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-
?
NADH + H+ + O2
NAD+ + H2O2
the enzyme is highly specific for NADH, no activity with NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
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?
NADH + H+ + O2
NAD+ + H2O2
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oxidizes specifically beta-NADH in the presence of molecular oxygen
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?
NADH + H+ + O2
NAD+ + H2O2
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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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NADH + H+ + O2
NAD+ + H2O2
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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
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?
additional information
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the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c
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?
additional information
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the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c
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beta-NADH + H+ + O2
beta-NAD+ + H2O2
NADH + H+ + O2
NAD+ + H2O2
beta-NADH + H+ + O2
beta-NAD+ + H2O2
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-
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?
beta-NADH + H+ + O2
beta-NAD+ + H2O2
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?
NADH + H+ + O2
NAD+ + H2O2
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NADH + H+ + O2
NAD+ + H2O2
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NADH + H+ + O2
NAD+ + H2O2
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme is highly specific for NADH, no activity with NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
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the enzyme is highly specific for NADH, no activity with NADPH
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?
NADH + H+ + O2
NAD+ + H2O2
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NADH + H+ + O2
NAD+ + H2O2
Nox-1 is a protective protein against oxygen toxicity
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?
NADH + H+ + O2
NAD+ + H2O2
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
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?
NADH + H+ + O2
NAD+ + H2O2
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidases, a H2O2-forming and a H2O-forming enzyme
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?
NADH + H+ + O2
NAD+ + H2O2
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?
NADH + H+ + O2
NAD+ + H2O2
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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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?
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FAD
flavoprotein
FAD
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a flavoprotein, contains 1.8 mol of non-covalently bound FAD per mol of native enzyme
FAD
contains 1 mol of FAD per monomer
FAD
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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
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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
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requires the presence of a flavin cofactor, showing a high specificity for FAD. The enzyme does not contain a flavin molecule
FAD
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requires the presence of a flavin cofactor, showing a high specificity for FAD. The enzyme is purified as an FAD-containing protein
FAD
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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
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NADH
no activity with NADPH
NADH
absolute specificity for NADH
NADH
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the enzyme is highly specific for NADH
NADH
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the enzyme is highly specific for NADH, little or no activity with NADPH
NADH
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the enzyme is highly specific for NADH, 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
NADH
-
NADPH can not act as the electron donor
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CuCl2
10 mM, 3-4fold stimulation
K3Fe(CN)6
10 mM, 3-4fold stimulation
Mg2+
-
12 mM, slight stimulation
Mg2+
0.1 mM, 130% stimulation
additional information
divalent cations are not required for activity
additional information
divalent cations are not required for activity
additional information
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divalent cations are not required for activity
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4-chloromercuribenzoate
0.1 mM, 40% inhibition
5,5'-dithiobis-(2-nitrobenzoate)
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1 mM, 7 min, 50% loss of activity
AgNO3
-
1 mM, 63% inhibition
ascorbate
1 mM, 81% inhibition
Ba2+
0.1 mM, 86% inhibition
Ca2+
0.1 mM, about 20% inhibition
CaCl2
10 mM, slightly increases activity
Cd(CH3CH2COO-)2
10 mM, slightly increases activity
Co2+
0.1 mM, 31% inhibition
CoCl2
10 mM, slightly increases activity
Cr2+
0.1 mM, 49% inhibition
Cu2+
0.1 mM, complete inhibition
CuSO4
-
1 mM, 1 h at 22°C, 85% remaining activity
cysteine
1 mM, 54% inhibition
dithiothreitol
2 mM, rapid decrease in activity to less than 10% of the activity
EGTA
10 mM, slightly increases activity
Fe2+
0.1 mM, 56% inhibition
FeSO4
-
1 mM, 1 h at 22°C, 56% remaining activity
Hg2+
0.1 mM, complete inhibition
hydrocortisone
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3 mM, 5% inhibition
MgCl2
-
1 mM, 1 h at 22°C, 93% remaining activity
Mn2+
0.1 mM, about 20% inhibition
MnCl2
10 mM, slightly increases activity
Ni2+
0.1 mM, 73% inhibition
NiCl2
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1 mM, 1 h at 22°C, 71% remaining activity
Quinacrine
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3 mM, 46% inhibition
Quinine
-
3 mM, 23% inhibition
SDS
0.5%, completely inhibits the reaction
Sn2+
0.1 mM, complete inhibition
sodium deoxycholate
0.5%, slightly decreases activity
Zn2+
0.1 mM, 53% inhibition
ZnSO4
-
1 mM, 1 h at 22°C, 69% remaining activity
CuCl2
-
1 mM, 58% inhibition
CuCl2
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3 mM, 60% inhibition
Guanidine-HCl
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-
HgCl2
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1 mM, 29% inhibition
HgCl2
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1 mM, 1 h at 22°C, 6% remaining activity
HgCl2
-
3 mM, 98% inhibition
Urea
-
-
ZnCl2
10 mM, slightly increases activity
ZnCl2
-
1 mM, 61% inhibition
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(NH4)2SO4
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250 mM, 10fold activation
2-mercaptoethanol
2 mM, stimulates up to 2fold
CHAPS
0.2-0.5%, increases activity about twofold
n-dodecyl beta-D-maltoside
0.5%, increases activity about twofold
p-chloromercuribenzoate
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1 mM, 1.9fold activation
Triton X-100
0.1-0.5%, increases activity about twofold
Tween 20
1.25%, increases activity about twofold
dithiothreitol
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5 mM, slight stimulation
dithiothreitol
2 mM, stimulates up to 2fold
dithiothreitol
1 mM, slight stimulation to 103%
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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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.
Cardiomyopathies
Myocardial Redox Hormesis Protects the Heart of Female Mice in Sepsis.
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
Myocardial Redox Hormesis Protects the Heart of Female Mice in Sepsis.
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.
Stroke
Role of neuronal NADPH oxidase 1 in the peri-infarct regions after stroke.
Thrombosis
Angiotensin II and nitric oxide interaction.
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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0.0037
beta-NADH
pH and temperature not specified in the publication
additional information
additional information
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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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0.00153
NADH
pH 7.0, 25°C
0.0075
NADH
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pH 7.0, 80°C
0.022
NADH
-
pH 8.8, 25°C
0.042
NADH
-
pH 7.8, 80°C
0.05
NADH
30°C, pH not specified in the publication
0.043
O2
-
pH 7.8, 80°C
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115
beta-NADH
pH and temperature not specified in the publication
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37
30°C, pH not specified in the publication
84
pH and temperature not specified in the publication
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4.5 - 5
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the activity decreases with pH in the range pH 4.5 to 9.8
6.5
-
assay at
7
assay at
8
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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
4.5 - 9.8
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the activity decreases with pH in the range pH 4.5 to 9.8
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 - 7.5
-
very active in the pH-range 6.5-7.5
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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30 - 58
-
the activity increases with the temperature, as tested from 30°C to 58°C
80
-
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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
30 - 70
-
activity at 30°C is about 40% of the maximal at 70°C
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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brenda
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SwissProt
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UniProt
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UniProt
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UniProt
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brenda
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UniProt
brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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malfunction
the lack of a significant effect on deletion of the genes from Streptococcus mutans suggests the presence of additional antioxidant proteins in this bacterium
physiological function
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although Pyrococcus furiosus is a strict anaerobe, it may tolerate oxygen to some extent. NOX1 may be involved in the response to oxygen at high temperatures
physiological function
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further investigation is required to conclude firmly if the purified NADH oxidase is part of an enzyme system that protects anaerobic Thermotoga hypogea from accidental exposure to O2
physiological function
Nox-1 is a protective protein against oxygen toxicity
physiological function
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration
physiological function
the fact that the expression of the Nox enzymes is not regulated suggests that they have some fundamental metabolic role, and not an occasional role during oxygen stress
physiological function
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further investigation is required to conclude firmly if the purified NADH oxidase is part of an enzyme system that protects anaerobic Thermotoga hypogea from accidental exposure to O2
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A0A401HR01_9EURY
449
0
49006
TrEMBL
-
A0A7J9PAA3_METMI
442
0
47592
TrEMBL
-
A0A7J9P3H2_METMI
442
0
47596
TrEMBL
-
A0A7W4Z169_9ACTN
441
0
46585
TrEMBL
-
A0A7J9NI76_METMI
442
0
47626
TrEMBL
-
A0A7J9S2U9_METMI
442
0
47605
TrEMBL
-
A0A7J9S0F8_METMI
442
0
47555
TrEMBL
-
A0A7J9NPS4_METMI
442
0
47553
TrEMBL
-
A0A7J9P3A6_METMI
442
0
47591
TrEMBL
-
A0A8B3S299_9EURY
448
0
47719
TrEMBL
-
A0A8B6FLI7_MYTGA
442
0
49234
TrEMBL
other Location (Reliability: 3 )
A0A8J7S4C5_METVO
459
0
49633
TrEMBL
-
A0A7J9NRP3_METMI
442
0
47484
TrEMBL
-
A0A2L1CC68_METMI
442
0
47598
TrEMBL
-
A0A7J9PDA7_METMI
442
0
47546
TrEMBL
-
A0A8B3S410_9EURY
452
1
49084
TrEMBL
-
A0A368TGI0_9EURY
469
0
49780
TrEMBL
-
A0A288Q678_9LACO
441
0
47388
TrEMBL
-
O29794_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
632
0
68706
TrEMBL
Mitochondrion (Reliability: 4 )
O29852_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
436
0
46964
TrEMBL
-
O29985_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
439
0
47979
TrEMBL
-
O58049_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
176
0
20073
TrEMBL
-
O66266_STRMG
510
0
55147
TrEMBL
-
NAOX_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
448
0
48876
Swiss-Prot
-
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152000
tetrameric enzyme form, gel filtration
178000
tetrameric enzyme form, gel filtration
22000
4 * 22000, SDS-PAGE
46000
-
1 * 54000 + 1 * 46000, SDS-PAGE
47000
x * 47000, SDS-PAGE
54000
-
1 * 54000 + 1 * 46000, SDS-PAGE
55196
x * 55196, calculated from sequence
56000
4 * 56000, SDS-PAGE
57000
-
2 * 57000, SDS-PAGE
94000
dimeric enzyme form, gel filtration
48000
2 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE
48000
4 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
50000
x * 50000, SDS-PAGE
68000
1 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE
68000
2 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE
70000
dimeric enzyme form, gel filtration
70000
-
1 * 70000, SDS-PAGE
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?
x * 47000, SDS-PAGE
?
x * 55196, calculated from sequence
?
-
x * 55196, calculated from sequence
-
dimer
2 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE
dimer
2 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
-
dimer
-
2 * 50000, SDS-PAGE
dimer
-
1 * 54000 + 1 * 46000, SDS-PAGE
homodimer
-
2 * 50000, SDS-PAGE
homodimer
-
2 * 50000, SDS-PAGE
-
homotetramer
4 * 22000, SDS-PAGE
homotetramer
-
4 * 22000, SDS-PAGE
-
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
-
monomer
1 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE
tetramer
4 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE
tetramer
4 * 56000, SDS-PAGE
tetramer
-
4 * 56000, SDS-PAGE
-
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5 - 8
37°C, 1 h, the enzyme retains full activity at pH 7.0, but activity declines following incubation at either acidic or alkaline pH
722881
6 - 10
-
1 h, stable
721365
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40
pH 7.0, 1 h, enzyme retains full activity
55
pH 7.0, 1 h, activity markedly decreases
60
30 min, enzyme retains 5% of its activity
83
pH 7.6, 40 min, the half-life of the recombinant enzyme is 12 min, the partially purified native enzyme has a half-life of 35 h
70
-
1 h, no significant loss of activity
70
-
8 h, no loss of activity
80
half-life: 40 min
80
-
1 h, about 30% loss of activity
90
-
100 min, 50% loss of activity
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apparently, the enzyme in the cell extract is more resistant to oxygen inactivation than the purified enzyme. Purified enzyme samples exposed to air exhibit a decrease in enzyme activity. The inactivation rate of NADH oxidase activity is dependent on oxygen concentration. The times required for the loss of 50% of the enzyme activity from the purified enzyme are about 20 min and 40 min for oxygen concentrations of 20% (v/v) and 1% (v/v), respectively. However, the times required for the loss of 50% of the enzyme activity from the cell extract aree about 60 min and 360 min for oxygen concentration of 20% (v/v) and 1% (v/v), respectively
-
722518
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-80°C, 6 months, enzyme retains full activity
4°C. pH 7.0, 1 week, activity decreases by 80%
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purified under strictly anaerobic conditions
-
-
-
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expression in Escherichi coli C41
expression in Escherichia coli
expression of the nox-1 gene in Escherichia coli using its own promoter
overexpressed in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
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expressed constitutively under strictly anaerobic conditions. The fact that the expression of the Nox enzymes is not regulated suggests that they have some fundamental metabolic role, and not an occasional role during oxygen stress
transcriptional analysis demonstrates that NOX1 is constitutively expressed regardless of the carbon source and a single promoter is identified 25 bp upstream of the nox1 gene by primer extension
-
aerobically induced
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synthesis
-
regeneration of NAD+ utilizing this enzyme made selective oxidation of mandelic acid or L-phenylalanine possible. This thermostable enzyme is expected to be applicable as a useful biocatalyst for NAD+ recycling
synthesis
the enzyme is applicable as a biocatalyst for NAD+ recycling
synthesis
-
regeneration of NAD+ utilizing this enzyme made selective oxidation of mandelic acid or L-phenylalanine possible. This thermostable enzyme is expected to be applicable as a useful biocatalyst for NAD+ recycling
-
synthesis
-
the enzyme is applicable as a biocatalyst for NAD+ recycling
-
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Case, C.L.; Rodriguez, J.R.; Mukhopadhyay, B.
Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii
Microbiology
155
69-79
2009
Methanocaldococcus jannaschii (Q58065), Methanocaldococcus jannaschii
brenda
Hirano, J.; Miyamoto, K.; Ohta, H.
Purification and characterization of thermostable H2O2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309
Appl. Microbiol. Biotechnol.
80
71-78
2008
Brevibacterium sp., Brevibacterium sp. KU1309
brenda
Yang, X.; Ma, K.
Purification and characterization of an NADH oxidase from extremely thermophilic anaerobic bacterium Thermotoga hypogea
Arch. Microbiol.
183
331-337
2005
Pseudothermotoga hypogea, Pseudothermotoga hypogea DSM 11164
brenda
Higuchi, M.; Shimada, M.; Matsumoto, J.; Yamamoto, Y.; Rhaman, A.; Kamio, Y.
Molecular cloning and sequence analysis of the gene encoding the H2O2-forming NADH oxidase from Streptococcus mutans
Biosci. Biotechnol. Biochem.
58
1603-1607
1994
Streptococcus mutans (O66266), Streptococcus mutans, Streptococcus mutans NCBI 11723 (O66266)
brenda
Koh, J.-U.; Chung, H.-J.; Chang, W.-Y.; Tanokura, M.; Kong, K.-H.
Discovery and characterization of a thermostable NADH oxidase from Pyrococcus horikoshii OT3
Bull. Korean Chem. Soc.
30
2984-2988
2009
Pyrococcus horikoshii (O58049), Pyrococcus horikoshii OT-3 (O58049)
-
brenda
Ward, D.E.; Donnelly, C.J.; Mullendore, M.E.; van der Oost, J.; de Vos W.M.; Crane, E.J. 3rd.
The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress
Eur. J. Biochem.
268
5816-5823
2001
Pyrococcus furiosus
brenda
Kengen, S.W.; van der Oost, J.; de Vos, W.M.
Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus
Eur. J. Biochem.
270
2885-2994
2003
Archaeoglobus fulgidus (O29794), Archaeoglobus fulgidus (O29985), Archaeoglobus fulgidus
brenda
Poole, L.B.; Higuchi, M.; Shimada, M.; Calzi, M.L.; Kamio, Y.
Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein
Free Radic. Biol. Med.
28
108-120
2000
Streptococcus mutans (O66266), Streptococcus mutans
brenda
Reed, D.W.; Millstein, J.; Hartzell, P.L.
H(2)O(2)-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus
J. Bacteriol.
183
7007-7016
2001
Archaeoglobus fulgidus (O29852), Archaeoglobus fulgidus
brenda
Yang, X.; Ma, K.
Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima
J. Bacteriol.
189
3312-3317
2007
Thermotoga maritima
brenda
Higuchi, M.; Shimada, M.; Yamamoto, Y.; Hayashi, T.; Koga, T.; Kamio, Y.
Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans
J. Gen. Microbiol.
139
2343-2351
1993
Streptococcus mutans (O66266), Streptococcus mutans NCBI 11723 (O66266)
brenda
Gomes, C.M.; Teixeira, M.
The NADH oxidase from the thermoacidophilic archaea Acidianus ambivalens: isolation and physicochemical characterisation
Biochem. Biophys. Res. Commun.
243
412-415
1998
Acidianus ambivalens, Acidianus ambivalens DSM 3772
brenda
Masullo, M.; Raimo, G.; Dello Russo, A.; Bocchini, V.; Bannister, J.V.
Purification and characterization of NADH oxidase from the archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus
Biotechnol. Appl. Biochem.
23
47-54
1996
Sulfolobus acidocaldarius, Saccharolobus solfataricus
brenda
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