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Information on EC 1.6.3.3 - NADH oxidase (H2O2-forming)

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EC Tree
     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.3 With oxygen as acceptor
                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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UNIPROT: O66266
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
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NADH
+
H+
+
O2
=
NAD+
+
H2O2
+
+
=
+
Synonyms
nox-1, noxb-1, noxa2, noxa-1, mj0649, mjnox, h2o2-forming nadh oxidase, af0395, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H2O2-forming NADH oxidase
-
H2O2-forming reduced nicotinamide adenine dinucleotide oxidase
-
PATHWAY SOURCE
PATHWAYS
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
0.1 mM, 130% stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
0.1 mM, 40% inhibition
ascorbate
1 mM, 81% inhibition
Ba2+
0.1 mM, 86% inhibition
Ca2+
0.1 mM, about 20% inhibition
Co2+
0.1 mM, 31% inhibition
Cr2+
0.1 mM, 49% inhibition
Cu2+
0.1 mM, complete inhibition
cysteine
1 mM, 54% inhibition
Fe2+
0.1 mM, 56% inhibition
Hg2+
0.1 mM, complete inhibition
Mn2+
0.1 mM, about 20% inhibition
Ni2+
0.1 mM, 73% inhibition
Sn2+
0.1 mM, complete inhibition
Zn2+
0.1 mM, 53% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
1 mM, slight stimulation to 103%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00153 - 0.05
NADH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
30°C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
pH 4.5: about 90% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
30°C; about 75% of maximal activity, 50°C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Nox-1 is a protective protein against oxygen toxicity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O66266_STRMG
510
0
55147
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220000
gel filtration
55196
x * 55196, calculated from sequence
56000
4 * 56000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55196, calculated from sequence
tetramer
4 * 56000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 6 months, enzyme retains full activity
4°C. pH 7.0, 1 week, activity decreases by 80%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the nox-1 gene in Escherichia coli using its own promoter
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aerobically induced
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team