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Information on EC 1.6.3.4 - NADH oxidase (H2O-forming)
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1.6.3.4 NADH oxidase (H2O-forming)IUBMB Comments
A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O-forming enzyme and a H2O2-forming enzyme (cf. EC 1.6.3.3, NADH oxidase (H2O2-forming)) .
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
nox-2, water-forming nadh oxidase, nicotinamide adenine dinucleotide oxidase, spnox, h2o-forming nadh oxidase, lrnox, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H2O-forming NADH oxidase
LrNox
NOX
Nox-2
NoxA
NoxE
water-forming NADH oxidase
YODC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 NADH + 2 H+ + O2 = 2 NAD+ + 2 H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NADH:oxygen oxidoreductase (H2O-forming)
A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O-forming enzyme and a H2O2-forming enzyme (cf. EC 1.6.3.3, NADH oxidase (H2O2-forming)) [1].
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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
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 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
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
-
-
?
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+ + oxidized methylene blue
NAD+ + reduced methylene blue
-
-
-
?
NADH + H+ + oxidized methylene blue
NAD+ + reduced methylene blue
Lactococcus cremoris MG1363
-
-
-
?
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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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
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 is involved detoxification of oxygen to water
-
-
?
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
Streptococcus mutans NCBI 11723 contains two distinct NADH oxidase, a H2O2-forming and a H2O-forming enzyme
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
flavoenzyme. Optimum FAD concentration for the LrNox is 0.01 mM, with 90% and 3% of maximum activity at 0.001 mM and 0.5 mM FAD, respectively. Enzyme activity decreases sharply with an increase in FAD concentration due to inhibition by FAD. More than 90% enzyme activity is lost when FAD concentration is increased from 0.01 to 0.3 mM
FAD
flavoprotein, contains 34 mol FAD per mol native enzyme. The NADH oxidase activity is not stimulated by the addition of free flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), or riboflavin to the reaction mixture (final concentrations were 0.1 mM)
NADH
the enzyme is highly specific for NADH, no activity with NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme does not require a metal cofactor for activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
optimum FAD concentration for the LrNox is 0.01 mM, with 90% and 3% of maximum activity at 0.001 mM and 0.5 mM FAD, respectively. Enzyme activity decreases sharply with an increase in FAD concentration due to inhibition by FAD. More than 90% enzyme activity is lost when FAD concentration is increased from 0.01 to 0.3 mM
additional information
no significant inhibition at 0.1 mM, Ba2+, Ni2+, Fe2+ and Zn2+. Cysteine (1 mM), 1% inhibition
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Aortic Aneurysm
Hyperhomocysteinemia during aortic aneurysm, a plausible role of epigenetics.
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.
Tuberculosis
AN ALLOSTERIC REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE OXIDASE FROM MYCOBACTERIUM TUBERCULOSIS.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 6
-
pH 4.6: 68% of maximal activity, pH 6.0: 54% of maximal activity
6 - 9.3
pH 6.0: about 60% of maximal activity, pH 9.3: about 50% of maximal activity
6.5 - 8.5
-
higher than 70% of the maximum activity at pH values of 6.58.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
-
the enzyme is not thermal-sensitive since there is an activity change of only 28% when the temperature varies in the range of 25°C to 70°C
30 - 50
30°C: about 60% of maximal activity, 50°C: about 65% of maximal activity
30 - 70
-
30°C: about 75% of maximal activity, 70°C: about 80% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Lactococcus cremoris MG1363
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the inability of the nox2 mutant to grow aerobically is mainly due to an underlying defect in fatty acid biosynthesis. NAD+ depletion in the nox2 mutant results in reduced acetyl-CoA production, which perturbs fatty acid biosynthesis and hence blocks growth in aerobiosis
metabolism
physiological function
metabolism
the enzyme can regulate the metabolism during aerobic fermentation in Saccharomyces cerevisiae, thereby protecting cells against several stresses
metabolism
Lactococcus cremoris MG1363
-
the enzyme can regulate the metabolism during aerobic fermentation in Saccharomyces cerevisiae, thereby protecting cells against several stresses
-
physiological function
the enzyme is essential for aerobic growth and oxidative stress resistance in conventional culture media. The enzyme facilitates adaptation of group B Streptococci to aerobic conditions encountered during infection
physiological function
the enzyme is involved in oxygen metabolism
physiological function
-
the enzyme is involved in oxygen metabolism
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FPRA1_CLOAB
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
392
0
44491
Swiss-Prot
-
FPRA2_CLOAB
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
400
0
45044
Swiss-Prot
-
B0NK28_CLOS5
Clostridium scindens (strain ATCC 35704 / DSM 5676 / VPI 13733 / 19)
399
0
45644
TrEMBL
-
A0A644XE94_9ZZZZ
391
0
44053
TrEMBL
other Location (Reliability: 2)
A0A645IMJ4_9ZZZZ
110
0
12325
TrEMBL
other Location (Reliability: 5)
A0A644XF48_9ZZZZ
390
0
44233
TrEMBL
other Location (Reliability: 1)
A0A645JAH5_9ZZZZ
80
0
8964
TrEMBL
other Location (Reliability: 2)
A0A645FE54_9ZZZZ
213
0
23746
TrEMBL
other Location (Reliability: 2)
A0A644UGE9_9ZZZZ
394
0
43599
TrEMBL
other Location (Reliability: 1)
A0A645I730_9ZZZZ
110
0
11896
TrEMBL
other Location (Reliability: 2)
A0A644U410_9ZZZZ
407
0
45990
TrEMBL
other Location (Reliability: 2)
A0A644ZMR1_9ZZZZ
296
0
32576
TrEMBL
other Location (Reliability: 2)
A0A644XBK6_9ZZZZ
445
0
49477
TrEMBL
other Location (Reliability: 2)
NAOX_LACLM
Lactococcus lactis subsp. cremoris (strain MG1363)
446
0
48872
Swiss-Prot
-
Q2WFW5_9FIRM
448
0
49293
TrEMBL
Secretory Pathway (Reliability: 5)
Q8E5N5_STRA3
Streptococcus agalactiae serotype III (strain NEM316)
456
0
49855
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
50000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of this protein are grown by sitting-drop variant of the vapour-diffusion method at 20°C in the presence of 34% polyethylene glycol monomethyl ether 2000, 0.1 M sodium acetate and 0.2 M ammonium sulfate at pH 5.4. They belong to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = 74.8, b = 95.7, c = 116.9 A, alpha = gamma = 90°, beta = 103.8°. The diffraction limit is 4.0 A
homology modeling and substrate docking, the nicotinamide ring of NADH extends vertically toward to re-face of coenzyme (FAD)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D251R
-
mutation improves the activity to 112%, 111%, and 244% of the wild-type at pH 6.5, pH 7.0, and pH 7.5, respectively. NADH has access to the substrate-binding site with a larger substrate loop due to the enhanced electrostatic repulsion between Arg251 and Arg243. In the D251R-NADH complex, the carboxyl of NADH additionally forms two hydrogen bonds with G154 due to the changed interaction of substrate and the residues in the catalytic sites, and the hydrogen bond with the oxygen of carbonyl in P295 is shortened from 2.9 to 2.0 A
D292A
-
mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity
G13A
-
mutant enzyme nearly loses all activity, also loses yellow color, indicating that the amino acid is important for activity
G169A
-
loses nearly 100% of its activity, indicating that G169 is important for NADH binding
K182R
-
the mutation slightly enhances NADH oxidase activity by approximately 10%
K184A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184D
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184F
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184G
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K184Q
-
the mutant shows reduced activity compared to the wild type enzyme
K184R
-
the mutation enhances NADH oxidase activity by approximately 50% and improves thermostability with 46.6 % longer half-life at 30°C
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 - 8
-
after incubation between pH 6.0 and 8.0 for 2 h, the enzyme maintains more than 90% of the whole activity
743220
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
60
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and HiTrap Blue column chromatography
Ni-NTA column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the T7 promoter-based plasmid pET28a to give pET28a-SpNox and then heterologously overexpressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21(DE3) cells
expressed in pyruvate decarboxylase-deficient Saccharomyces cerevisiae strain SOS2
-
expressed in Saccharomyces cerevisiae strain BY4741 and Clostridium acetobutylicum strain 428
overexpression in Lactococcus lactis strains, plasmid vector pNZ8020 under the control of the Lactococcus lactis nisA promoter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aerobically induced
the expression of noxA is strongly upregulated within 10 min after the growth conditions are altered to a microoxic state
the expression of noxA is strongly upregulated within 10 min after the growth conditions are altered to a microoxic state
the expression of noxA is strongly upregulated within 10 min after the growth conditions are altered to a microoxic state
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
the enzyme may prove to be useful for NAD+ regeneration in the production rare L--sugars such as L-ribose, L-ribulose, and L-xylulose
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Release 2023.1 (January 2023)
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