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Enzyme Nomenclature
Information on EC 1.6.3.4 - NADH oxidase (H2O-forming)
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.6.3.4
-
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RECOMMENDED NAME
GeneOntology No.
NADH oxidase (H2O-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 NADH + 2 H+ + O2 = 2 NAD+ + 2 H2O
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-
-
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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
physiological function
physiological function
-
the enzyme is involved in oxygen metabolism
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
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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
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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
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-
?
2 NADH + H+ + O2
NAD+ + 2 H2O
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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
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the enzyme is highly specific for NADH, no activity with NADPH
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
flavoprotein, contains 3–4 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)
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
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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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INHIBITORS
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
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no significant inhibtion 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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KM VALUE [mM]
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
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pH 6.0: about 60% of maximal activity, pH 9.3: about 50% of maximal activity
6.5 - 8.5
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higher than 70% of the maximum activity at pH values of 6.5–8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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30°C: about 60% of maximal activity, 50°C: about 65% of maximal activity
30 - 70
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30°C: about 75% of maximal activity, 70°C: about 80% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
100000
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SUBUNITS
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
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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
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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
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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)
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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
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the expression of noxA is strongly upregulated within 10 min after the growth conditions are altered to a microoxic state
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-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C42A
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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.6.3.4)
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