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2 NADH + 2 H+ + O2
2 NAD+ + 2 H2O
2 NADH + H+ + O2
NAD+ + 2 H2O
BNAH + H+ + O2
BNA+ + H2O
MNAH + H+ + O2
MNA+ + H2O
NADH + H+ + O2
NAD+ + H2O
NADH + H+ + oxidized methylene blue
NAD+ + reduced methylene blue
additional information
?
-
2 NADH + 2 H+ + O2
2 NAD+ + 2 H2O
-
-
-
-
?
2 NADH + 2 H+ + O2
2 NAD+ + 2 H2O
-
-
-
?
2 NADH + 2 H+ + O2
2 NAD+ + 2 H2O
-
-
-
-
?
2 NADH + 2 H+ + O2
2 NAD+ + 2 H2O
-
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
the enzyme is involved detoxification of oxygen to water
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
the enzyme can catalyze electron transfers from NADH to ferricyanide, 2,6-dichloroindophenol, and menadione, although the activities with these acceptors are extremely low relative to O2. Thus, O2 must be a natural electron acceptor for this enzyme
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
the enzyme is involved detoxification of oxygen to water
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
the enzyme can catalyze electron transfers from NADH to ferricyanide, 2,6-dichloroindophenol, and menadione, although the activities with these acceptors are extremely low relative to O2. Thus, O2 must be a natural electron acceptor for this enzyme
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
the enzyme is highly specific for NADH, no activity with NADPH. O2 is the preferred electron acceptor, in addition FAD and, very slowly, one-electron acceptors are reduced. NO formation of H2O2
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidase, a H2O2-forming and a H2O-forming enzyme
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidase, a H2O2-forming and a H2O-forming enzyme
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
-
-
-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
-
no production of H2O2
-
-
?
BNAH + H+ + O2
BNA+ + H2O
i.e. N-benzyl-1,4-dihydronicotinamide
-
-
?
BNAH + H+ + O2
BNA+ + H2O
i.e. N-benzyl-1,4-dihydronicotinamide
-
-
?
MNAH + H+ + O2
MNA+ + H2O
i.e. N-methyl-1,4-dihydronicotinamide
-
-
?
MNAH + H+ + O2
MNA+ + H2O
i.e. N-methyl-1,4-dihydronicotinamide
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + O2
NAD+ + H2O
-
-
-
-
?
NADH + H+ + oxidized methylene blue
NAD+ + reduced methylene blue
-
-
-
?
NADH + H+ + oxidized methylene blue
NAD+ + reduced methylene blue
-
-
-
?
additional information
?
-
-
no activity with NADPH
-
-
?
additional information
?
-
-
no activity with NADPH
-
-
?
additional information
?
-
NADPH can be recognized as a substrate by the enzyme, though the specific activity is only about 2% compared to NADH
-
-
?
additional information
?
-
-
NADPH can be recognized as a substrate by the enzyme, though the specific activity is only about 2% compared to NADH
-
-
?
additional information
?
-
NADPH can be recognized as a substrate by the enzyme, though the specific activity is only about 2% compared to NADH
-
-
?
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Aortic Aneurysm
Hyperhomocysteinemia during aortic aneurysm, a plausible role of epigenetics.
Arthritis
Redox-mediated angiogenesis in the hypoxic joint of inflammatory arthritis.
Arthritis, Experimental
Redox-mediated angiogenesis in the hypoxic joint of inflammatory arthritis.
Carcinoma
Upregulation of NOX-2 and Nrf-2 Promotes 5-Fluorouracil Resistance of Human Colon Carcinoma (HCT-116) Cells.
Colorectal Neoplasms
Upregulation of NOX-2 and Nrf-2 Promotes 5-Fluorouracil Resistance of Human Colon Carcinoma (HCT-116) Cells.
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.
Dengue
Differential expression of NADPH oxidase-2 (Nox-2) and nuclear factor-erythroid 2-related factor 2 (Nrf2) transcripts in peripheral blood mononuclear cells isolated from dengue patients.
Hematuria
Melatonin treatment further improves adipose-derived mesenchymal stem cell therapy for acute interstitial cystitis in rat.
Hypertension
Brain-targeted Angiotensin-converting enzyme 2 overexpression attenuates neurogenic hypertension by inhibiting cyclooxygenase-mediated inflammation.
Hypertension
Ethyl Acetate Fraction of Lannea microcarpa Engl. and K. Krause (Anacardiaceae) Trunk Barks Corrects Angiotensin II-Induced Hypertension and Endothelial Dysfunction in Mice.
Hypertension
The inflammatory aspect of the microcirculation in hypertension: oxidative stress, leukocytes/endothelial interaction, apoptosis.
Hypothyroidism
Hypothyroidism and Oxidative Stress: Differential Effect on the Heart of Virgin and Pregnant Rats.
Infections
Differential expression of NADPH oxidase-2 (Nox-2) and nuclear factor-erythroid 2-related factor 2 (Nrf2) transcripts in peripheral blood mononuclear cells isolated from dengue patients.
Infections
The Group B Streptococcus NADH oxidase Nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence.
Myocardial Infarction
Enhanced NOX-2 derived oxidative stress in offspring of patients with early myocardial infarction.
Neoplasms
ENOX2 (or tNOX): a new and old molecule with cancer activity involved in tumor prevention and therapy.
Neoplasms
Punicalagin and (-)-Epigallocatechin-3-Gallate Rescue Cell Viability and Attenuate Inflammatory Responses of Human Epidermal Keratinocytes Exposed to Airborne Particulate Matter PM10.
Neoplasms
Upregulation of NOX-2 and Nrf-2 Promotes 5-Fluorouracil Resistance of Human Colon Carcinoma (HCT-116) Cells.
Non-alcoholic Fatty Liver Disease
LSEC Fenestrae Are Preserved Despite Pro-inflammatory Phenotype of Liver Sinusoidal Endothelial Cells in Mice on High Fat Diet.
Obesity
Effect of obesity reduction on preservation of heart function and attenuation of left ventricular remodeling, oxidative stress and inflammation in obese mice.
Pancreatic Neoplasms
Synthetic 8-hydroxydeoxyguanosine inhibited metastasis of pancreatic cancer through concerted inhibitions of ERM and Rho-GTPase.
Parkinson Disease
Microglial Cells Are Involved in the Susceptibility of NADPH Oxidase Knockout Mice to 6-Hydroxy-Dopamine-Induced Neurodegeneration.
Pneumonia
Acute lung injury leads to depression-like symptoms through upregulation of neutrophilic and neuronal NADPH oxidase signaling in a murine model.
Pneumonia
The Expression of NOX From Synthetic Promoters Reveals an Important Role of the Redox Status in Regulating Secondary Metabolism of Saccharopolyspora erythraea.
Sepsis
Tolerizing CTL by Sustained Hepatic PD-L1 Expression Provides a New Therapy Approach in Mouse Sepsis.
Shock, Septic
Myocardial Redox Hormesis Protects the Heart of Female Mice in Sepsis.
Tuberculosis
AN ALLOSTERIC REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE OXIDASE FROM MYCOBACTERIUM TUBERCULOSIS.
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Kawasaki, S.; Watamura, Y.; Ono, M.; Watanabe, T.; Takeda, K.; Niimura, Y.
Adaptive responses to oxygen stress in obligatory anaerobes Clostridium acetobutylicum and Clostridium aminovalericum
Appl. Environ. Microbiol.
71
8442-8550
2005
no activity in Clostridium acetobutylicum, Anaerocolumna aminovalerica (Q2WFW5), Anaerocolumna aminovalerica, Anaerocolumna aminovalerica NRIC0223 (Q2WFW5)
brenda
Kawasaki, S.; Ishikura, J.; Chiba, D.; Nishino, T.; Niimura, Y.
Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria
Arch. Microbiol.
181
324-330
2004
Anaerocolumna aminovalerica (Q2WFW5), Anaerocolumna aminovalerica, Anaerocolumna aminovalerica NRIC0223 (Q2WFW5)
brenda
Gao, H.; Tiwari, M.K.; Kang, Y.C.; Lee, J.K.
Characterization of H2O-forming NADH oxidase from Streptococcus pyogenes and its application in L-rare sugar production
Bioorg. Med. Chem. Lett.
22
1931-1935
2012
Streptococcus pyogenes
brenda
Matsumoto, J.; Higuchi, M.; Shimada, M.; Yamamoto, Y.; Kamio, Y.
Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans
Biosci. Biotechnol. Biochem.
60
39-43
1996
Streptococcus mutans (Q54453), Streptococcus mutans, Streptococcus mutans NCBI 11723 (Q54453)
brenda
Zhang, Y.W.; Tiwari, M.K.; Gao, H.; Dhiman, S.S.; Jeya, M.; Lee, J.K.
Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus
Enzyme Microb. Technol.
50
255-262
2012
Lacticaseibacillus rhamnosus, Lacticaseibacillus rhamnosus ATCC 53103
brenda
Schmidt, H.L.; Stcklein, W.; Danzer, J.; Kirch, P.; Limbach, B.
Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis
Eur. J. Biochem.
156
149-155
1986
Enterococcus faecalis
brenda
Lopez de Felipe, F.; Kleerebezem, M.; de Vos, W.M.; Hugenholtz, J.
Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase
J. Bacteriol.
180
3804-3808
1998
Streptococcus mutans (Q8E5N5), Streptococcus mutans
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 (Q54453), Streptococcus mutans NCBI 11723 (Q54453)
brenda
Heux, S.; Cachon, R.; Dequin, S.
Cofactor engineering in Saccharomyces cerevisiae: Expression of a H2O-forming NADH oxidase and impact on redox metabolism
Metab. Eng.
8
303-314
2006
Lactococcus lactis (A2RIB7), Lactococcus lactis, Lactococcus lactis MG1363 (A2RIB7)
brenda
Yamamoto, Y.; Pargade, V.; Lamberet, G.; Gaudu, P.; Thomas, F.; Texereau, J.; Gruss, A.; Trieu-Cuot, P.; Poyart, C.
The Group B Streptococcus NADH oxidase Nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence
Mol. Microbiol.
62
772-785
2006
Streptococcus agalactiae (Q8E5N5)
brenda
Kuzu, M.; Niefind, K.; Hummel, W.; Schomburg, D.
Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis
Acta Crystallogr. Sect. F
61
528-530
2005
Levilactobacillus brevis (Q8KRG4)
brenda
Gao, H.; Tiwari, M.K.; Singh, R.K.; Sung, B.H.; Kim, S.C.; Lee, J.K.
Role of surface residue 184 in the catalytic activity of NADH oxidase from Streptococcus pyogenes
Appl. Microbiol. Biotechnol.
98
7081-7088
2014
Streptococcus pyogenes
brenda
Kim, J.W.; Seo, S.O.; Zhang, G.C.; Jin, Y.S.; Seo, J.H.
Expression of Lactococcus lactis NADH oxidase increases 2,3-butanediol production in Pdc-deficient Saccharomyces cerevisiae
Biores. Technol.
191
512-519
2015
Lactococcus cremoris, Lactococcus cremoris MG1363
brenda
Yan, M.; Yin, W.; Fang, X.; Guo, J.; Shi, H.
Characteristics of a water-forming NADH oxidase from Methanobrevibacter smithii, an archaeon in the human gut
Biosci. Rep.
36
e00410
2016
Methanobrevibacter smithii, Methanobrevibacter smithii ATCC 35061
brenda
Shi, X.C.; Zou, Y.N.; Chen, Y.; Zheng, C.; Li, B.B.; Xu, J.H.; Shen, X.N.; Ying, H.J.
A water-forming NADH oxidase regulates metabolism in anaerobic fermentation
Biotechnol. Biofuels
9
103
2016
Lactococcus cremoris (A2RIB7), Lactococcus cremoris MG1363 (A2RIB7)
brenda
Shi, X.; Zou, Y.; Chen, Y.; Zheng, C.; Ying, H.
Overexpression of a water-forming NADH oxidase improves the metabolism and stress tolerance of Saccharomyces cerevisiae in aerobic fermentation
Front. Microbiol.
7
1427
2016
Lactococcus cremoris (A2RIB7), Lactococcus cremoris MG1363 (A2RIB7)
brenda
Zhang, G.C.; Turner, T.L.; Jin, Y.S.
Enhanced xylose fermentation by engineered yeast expressing NADH oxidase through high cell density inoculums
J. Ind. Microbiol. Biotechnol.
44
387-395
2017
Lactococcus cremoris (A2RIB7), Lactococcus cremoris MG1363 (A2RIB7)
brenda
Zhang, X.; Zhang, R.; Bao, T.; Rao, Z.; Yang, T.; Xu, M.; Xu, Z.; Li, H.; Yang, S.
The rebalanced pathway significantly enhances acetoin production by disruption of acetoin reductase gene and moderate-expression of a new water-forming NADH oxidase in Bacillus subtilis
Metab. Eng.
23
34-41
2014
Bacillus subtilis, Bacillus subtilis 168
brenda
Bae, S.J.; Kim, S.; Hahn, J.S.
Efficient production of acetoin in Saccharomyces cerevisiae by disruption of 2,3-butanediol dehydrogenase and expression of NADH oxidase
Sci. Rep.
6
27667
2016
Lactococcus cremoris (A2RIB7), Lactococcus cremoris MG1363 (A2RIB7)
brenda
Nowak, C.; Beer, B.; Pick, A.; Roth, T.; Lommes, P.; Sieber, V.
A water-forming NADH oxidase from Lactobacillus pentosus suitable for the regeneration of synthetic biomimetic cofactors
Front. Microbiol.
6
957
2018
Lactiplantibacillus pentosus (F6IXY6), Lactiplantibacillus pentosus, Lactiplantibacillus pentosus MP-10 (F6IXY6)
brenda
Zhou, Q.; Gao, J.; Zhang, Y.W.
Optimal pH shift of the NADH oxidase from Lactobacillus rhamnosus with a single mutation
Biotechnol. Lett.
43
1413-1420
2021
Lacticaseibacillus rhamnosus
brenda
Li, F.L.; Shi, Y.; Zhang, J.X.; Gao, J.; Zhang, Y.W.
Cloning, expression, characterization and homology modeling of a novel water-forming NADH oxidase from Streptococcus mutans ATCC 25175
Int. J. Biol. Macromol.
113
1073-1079
2018
Streptococcus mutans, Streptococcus mutans ATCC 25175
brenda