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Information on EC 1.7.1.15 - nitrite reductase (NADH) for references in articles please use BRENDA:EC1.7.1.15
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EC Tree
IUBMB Comments An iron-sulfur flavoprotein (FAD) containing siroheme. This prokaryotic enzyme is specific for NADH. In addition to catalysing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyse the 2-electron reduction of hydroxylamine to ammonia. cf. EC 1.7.1.4, nitrite reductase [NAD(P)H].
The enzyme appears in viruses and cellular organisms
Synonyms
nadh-dependent nitrite reductase, nasde, assimilatory nadh-nitrite reductase, nadh-dependent nitrite oxidoreductase,
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assimilatory NADH-nitrite reductase
assimilatory nitrite reductase
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ambiguous
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NADH-dependent nitrite oxidoreductase
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NADH-dependent nitrite reductase
NADH-nitrite oxidoreductase
NADH:nitrite oxidoreductase
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nitrite reductase (reduced nicotinamide adenine dinucleotide)
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assimilatory NADH-nitrite reductase
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assimilatory NADH-nitrite reductase
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NADH-dependent nitrite reductase
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NADH-dependent nitrite reductase
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NADH-dependent nitrite reductase
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NADH-dependent nitrite reductase
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NADH-nitrite oxidoreductase
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NADH-nitrite oxidoreductase
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NasB protein
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nasD
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gene name
NasDE
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nasE
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gene name
nirB
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gene name
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nirD
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gene name
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nirD
functional subunit of the active enzyme
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NH3 + 3 NAD+ + 2 H2O = nitrite + 3 NADH + 5 H+
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ammonia:NAD+ oxidoreductase
An iron-sulfur flavoprotein (FAD) containing siroheme. This prokaryotic enzyme is specific for NADH. In addition to catalysing the 6-electron reduction of nitrite to ammonia, the enzyme from Escherichia coli can also catalyse the 2-electron reduction of hydroxylamine to ammonia. cf. EC 1.7.1.4, nitrite reductase [NAD(P)H].
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2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
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horse heart cytochrome c + NADH + H+
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hydroxylamine + NADH + H+
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K3Fe(CN)6 + NADH + H+
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NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
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nitrite + NADH + H+
ammonia + NAD+ + H2O
nitrite + reduced benzyl viologen
ammonia + oxidized benzyl viologen
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
additional information
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nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
NADH is the best acceptor
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nitrite + NADH + H+
ammonia + NAD+ + H2O
NADH is the best acceptor
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nitrite + reduced benzyl viologen
ammonia + oxidized benzyl viologen
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nitrite + reduced benzyl viologen
ammonia + oxidized benzyl viologen
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nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
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nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
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nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
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additional information
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NirB, NirD polypeptides are essential for NADH-dependent nitrite reductase activity
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additional information
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NADPH is not an effcient electron donor
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additional information
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NADPH is not an effcient electron donor
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additional information
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NADPH is not an effcient electron donor
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additional information
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NADPH is not an effcient electron donor
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nitrite + NADH + H+
ammonia + NAD+ + H2O
nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
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nitrite + NADH + H+
ammonia + NAD+ + H2O
P0A9I8
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nitrite + NADH + H+
ammonia + NAD+ + H2O
Q6WRS9
NADH is the best acceptor
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nitrite + NADH + H+
ammonia + NAD+ + H2O
Q6WRS9
NADH is the best acceptor
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additional information
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the enzyme does not contain FMN
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FAD
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FAD
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the enzyme contains one non-covalently bound FAD molecule
Fe-S center
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Fe-S center
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the enzyme contains 5 Fe atoms and 4 acid-labile S atoms per subunit
NADH
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siroheme
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Iron
contains 2.8 mol iron per mol of protein
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2,2'-dipyridyl
68% inhibition at 2 mM
azide
36% inhibition at 2 mM
Cyanate
27% inhibition at 2 mM
cyanide
69% inhibition at 2 mM
dithioerythritol
52% inhibition at 2 mM
KCN
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although 1 mM KCN completely inhibits hydroxylamine reduction, it does not inhibit the reduction of K3Fe(CN)6 and only decreases the rate of cytochrome c reduction by 12%
NAD+
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NAD+ shows mixed product inhibition with respect to NADH and mixed or uncompetitive inhibition with respect to hydroxylamine
nitrite
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nitrite decrease the rate of NADH-dependent reduction of cytochrome c by 77% and that of Fe(CN)63- by 90%
o-phenanthroline
72% inhibition at 2 mM
p-chloromercuribenzoate
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the reduction of cytochrome c, K3Fe(CN)6 and hydroxylamine is completely inhibited (more than 99%) by 0.02 mM p-chloromercuribenzoate
p-hydroxymercurybenzoate
48% inhibition at 2 mM
additional information
the activity of the His6-tagged NasB protein is unaffected by thiocyanate
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additional information
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the activity of the His6-tagged NasB protein is unaffected by thiocyanate
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NAD+
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the apparent maximum velocity with NADH as varied substrate increases as the NAD+ concentration increases from 0.05 to 0.7 mM with 1 mM nitrite or 100 mM hydroxylamine as oxidized substrate
NAD+
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at 0.5 mM NAD+, the apparent maximum velocity is 2.3times higher for 0.1 mM cytochrome c as substrate than for 100 mM hydroxylamine
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0.0039
cytochrome c
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apparent value, at pH 8.0 and 30°C
2.91
hydroxylamine
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apparent value, at pH 8.0 and 30°C
0.1
K3Fe(CN)6
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apparent value, at pH 8.0 and 30°C
0.02
NADH
at pH 9.0 and 30°C
0.0488
NADH
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with cytochrome c as cosubstrate, apparent value, at pH 8.0 and 30°C
0.011
nitrite
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apparent value, at pH 8.0 and 30°C
0.5
nitrite
at pH 9.0 and 30°C
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0.052
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crude extract, at pH 8.0 and 30°C
2
purified enzyme, at pH 9.0 and 30°C
62.4
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after 121fold purification, at pH 8.0 and 30°C
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brenda
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brenda
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UniProt
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UniProt
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brenda
NirD polypeptide
UniProt
brenda
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brenda
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brenda
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brenda
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12000
x * 12000, NirD polypeptide, SDS-PAGE
86600
x * 86600, calculated from amino acid sequence
88000
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x * 88000, apoprotein, SDS-PAGE
88000
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2 * 88000, SDS-PAGE
88000
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x * 88000, SDS-PAGE
90000
x * 90000, His6-tagged enzyme, SDS-PAGE
90000
x * 90000, NirB polypeptide, SDS-PAGE
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homodimer
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2 * 88000, SDS-PAGE
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x * 88000, apoprotein, SDS-PAGE
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x * 12000, NirD polypeptide, SDS-PAGE; x * 90000, NirB polypeptide, SDS-PAGE
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x * 86600, calculated from amino acid sequence; x * 90000, His6-tagged enzyme, SDS-PAGE
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x * 86600, calculated from amino acid sequence; x * 90000, His6-tagged enzyme, SDS-PAGE
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4 - 30
the nitrite reductase activities of concentrated mixtures prepared on ice do not increase during subsequent incubation at 30°C or at 4°C
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1 mM nitrite and 5O mM hydroxylamine are equally effective in decreasing the loss of activity after 24h at 40°C from 40% to 10%. No increase in catalytic activity is detected when enzyme is pre-incubated for 15 min with either of these substrates, even when NAD+ is omitted from the assay mixture
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ammonium sulfate precipitation
DEAE-cellulose column chromatography
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Ni-NTA column chromatography
purified in the presence of 1 mM NO2- and 0.01 mM FAD by ammonium sulfate precipitation, DEAE-cellulose column chromatography, DEAE-Sephadex gel filtration, and Sephadex G-25 gel filtration
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expressed in Escherichia coli JCB323 cells
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expressed in Escherichia coli JM109 cells
expressed in Escherichia coli strain JCB387
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gene expression is co-ordinately repressed by oxygen
gene expression is induced during anaerobic growth
under conditions of oxygen limitation, nasDEF expression and nitrite reductase activity are significantly induced. ResDE is mainly (if not exclusively) responsible for nasDEF expression during anaerobic growth regardless of nitrogen sources
under conditions of oxygen limitation, nasDEF expression and nitrite reductase activity are significantly induced. ResDE is mainly (if not exclusively) responsible for nasDEF expression during anaerobic growth regardless of nitrogen sources
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under conditions of oxygen limitation, nasDEF expression and nitrite reductase activity are significantly induced. ResDE is mainly (if not exclusively) responsible for nasDEF expression during anaerobic growth regardless of nitrogen sources
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MacDonald, H.; Cole, J.
Molecular cloning and functional analysis of the cysG and nirB genes of Escherichia coli K12, two closely-linked genes required for NADH-dependent nitrite reductase activity
Mol. Gen. Genet.
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328-334
1985
Escherichia coli
brenda
Cammack, R.; Jackson, R.H.; Cornish-Bowden, A.; Cole, J.A.
Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12
Biochem. J.
207
333-339
1982
Escherichia coli
brenda
Jackson, R.H.; Cole, J.A.; Cornish-Bowden, A.
The steady-state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12
Biochem. J.
199
171-178
1981
Escherichia coli
brenda
Jackson, R.H.; Cornish-Bowden, A.; Cole, J.A.
Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12
Biochem. J.
193
861-867
1981
Escherichia coli
brenda
Nakano, M.M.; Hoffmann, T.; Zhu, Y.; Jahn, D.
Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE
J. Bacteriol.
180
5344-5350
1998
Bacillus subtilis, Bacillus subtilis JH642
brenda
Olmo-Mira, M.F.; Cabello, P.; Pino, C.; Martinez-Luque, M.; Richardson, D.J.; Castillo, F.; Roldan, M.D.; Moreno-Vivian, C.
Expression and characterization of the assimilatory NADH-nitrite reductase from the phototrophic bacterium Rhodobacter capsulatus E1F1
Arch. Microbiol.
186
339-344
2006
Rhodobacter capsulatus (Q6WRS9), Rhodobacter capsulatus, Rhodobacter capsulatus E1F1 (Q6WRS9), Rhodobacter capsulatus E1F1
brenda
Jackson, R.H.; Cole, J.A.; Cornish-Bowden, A.
The steady state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12. The reduction of single-electron acceptors
Biochem. J.
203
505-510
1982
Escherichia coli
brenda
Harborne, N.R.; Griffiths, L.; Busby, S.J.; Cole, J.A.
Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon
Mol. Microbiol.
6
2805-2813
1992
Escherichia coli, Escherichia coli (P0A9I8)
brenda
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1.7.1.15 nitrite reductase (NADH)
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