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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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nadh-dependent nitrite reductase, nirbd, nadh-nitrite reductase, nasde, assimilatory nadh-nitrite reductase, nadh-dependent nitrite oxidoreductase,
more
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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 reductase
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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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assimilatory NADH-nitrite reductase
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assimilatory NADH-nitrite reductase
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BMWSH_4089
A0A8D4BLJ9; A0A8D4BRF4
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BMWSH_4089
A0A8D4BLJ9; A0A8D4BRF4
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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
A0A8D4BLJ9; A0A8D4BRF4
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NasB
A0A8D4BLJ9; A0A8D4BRF4
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NasB protein
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nasD
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NasDE
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nasE
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nasE
A0A8D4BLJ9; A0A8D4BRF4
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nasE
A0A8D4BLJ9; A0A8D4BRF4
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nirB
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NirBD
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nirD
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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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?
ferricytochrome c + NADH + H+
ferrocytochrome c + NAD+
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r
horse heart cytochrome c + NADH + H+
?
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-
?
hydroxylamine + NADH + H+
?
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-
-
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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 + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
nitrite + NADH + H+
ammonia + NAD+ + H2O
nitrite + NADH + H+
nitrite + NAD+ + H2O
nitrite + reduced benzyl viologen
ammonia + oxidized benzyl viologen
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
nitrite + reduced methyl viologen
NH3 + oxidized methyl viologen
additional information
?
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nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
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?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
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-
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?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
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-
-
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?
nitrite + NADH + H+
ammonia + NAD+ + H2O
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-
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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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-
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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 + NADH + H+
nitrite + NAD+ + H2O
A0A8D4BLJ9; A0A8D4BRF4
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?
nitrite + NADH + H+
nitrite + NAD+ + H2O
A0A8D4BLJ9; A0A8D4BRF4
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-
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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
A0A8D4BLJ9; A0A8D4BRF4
the optimum electron donor is methyl viologen plus Na2S2O4
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-
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
A0A8D4BLJ9; A0A8D4BRF4
the optimum electron donor is methyl viologen plus Na2S2O4
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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
NH3 + oxidized methyl viologen
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methyl viologen is the best in vitro electron donor
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?
nitrite + reduced methyl viologen
NH3 + oxidized methyl viologen
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methyl viologen is the best in vitro electron donor
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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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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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?
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nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
nitrite + NADH + H+
ammonia + NAD+ + H2O
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
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?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
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?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 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
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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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?
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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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Fe2+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 226% of initial activity
Fe3+
-
131.97% activity at 5 mM
Iron
contains 2.8 mol iron per mol of protein
Mn2+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 110% of initial activity
Zn2+
-
126.21% activity at 5 mM
Zn2+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 113% of initial activity
additional information
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Mg2+ and Mn2+ have no evident effects on enzyme activity
additional information
A0A8D4BLJ9; A0A8D4BRF4
not inhibitory nor activating: Ba2+, EDTA
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2,2'-dipyridyl
68% inhibition at 2 mM
azide
36% inhibition at 2 mM
Cyanate
27% 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%
Mg2+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 82% of initial activity
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
Al3+
-
87.62% residual activity at 5 mM
Al3+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 84% of initial activity
Ca2+
-
43.78% residual activity at 5 mM
Ca2+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 80% of initial activity
Cu2+
-
65.3% residual activity at 5 mM
Cu2+
A0A8D4BLJ9; A0A8D4BRF4
1 mM, 54% initial activity
cyanide
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20.75% residual activity at 1 mM
cyanide
69% inhibition at 2 mM
additional information
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dithiothreitol and EDTA have no evident effects on enzyme activity
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additional information
A0A8D4BLJ9; A0A8D4BRF4
not inhibitory nor activating: Ba2+, EDTA
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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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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
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
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Tuberculosis
Crystal structure of NirD, the small subunit of the nitrite reductase NirBD from Mycobacterium tuberculosis, at 2.0 Å resolution.
Tuberculosis
Nitrite Reductase NirBD Is Induced and Plays an Important Role during In Vitro Dormancy of Mycobacterium tuberculosis.
Tuberculosis
The roles of the nitrate reductase NarGHJI, the nitrite reductase NirBD and the response regulator GlnR in nitrate assimilation of Mycobacterium tuberculosis.
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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
0.0103
nitrite
N-terminal plus C-terminal fragment, pH 7, 22°C
0.011
nitrite
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apparent value, at pH 8.0 and 30°C
0.0137
nitrite
N-terminal fragment, pH 7, 22°C
0.0353
nitrite
N-terminal plus C-terminal fragment, pH 7.5, 22°C
0.0355
nitrite
N-terminal fragment, pH 7.5, 22°C
0.5
nitrite
at pH 9.0 and 30°C
3.1
nitrite
A0A8D4BLJ9; A0A8D4BRF4
pH 7.1, 30°C
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1.2
nitrite
N-terminal plus C-terminal fragment, pH 7, 22°C
1.8
nitrite
N-terminal fragment, pH 7, 22°C
19.8
nitrite
N-terminal fragment, pH 7.5, 22°C
137.5
nitrite
N-terminal plus C-terminal fragment, pH 7.5, 22°C
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0.052
-
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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6.5
A0A8D4BLJ9; A0A8D4BRF4
-
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5 - 7
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the enzyme exhibits 95 % of its maximum activity at pH 6.5. At pH 5.0 and 7.0, it remains over 80% relative activity
6.8
A0A8D4BLJ9; A0A8D4BRF4
95% of maximum activity
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30
-
over 93% activity is retained at 40°C. At 20 and 50°C, the enzyme retains more than 73 and 66% activity, respectively
30
A0A8D4BLJ9; A0A8D4BRF4
-
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35
A0A8D4BLJ9; A0A8D4BRF4
95% of maximum activity
80
A0A8D4BLJ9; A0A8D4BRF4
50% of maximum activity
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5.7
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subunit nirD, calculated from amino acid sequence
6.3
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subunit nirB, calculated from amino acid sequence
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brenda
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brenda
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brenda
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brenda
A0A8D4BLJ9 i.e subunit NasE, A0A8D4BRF4 i.e. electron transfer subunit NasB
A0A8D4BLJ9; A0A8D4BRF4
UniProt
brenda
A0A8D4BLJ9 i.e subunit NasE, A0A8D4BRF4 i.e. electron transfer subunit NasB
A0A8D4BLJ9; A0A8D4BRF4
UniProt
brenda
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UniProt
brenda
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UniProt
brenda
isoform Nia1, cf. EC 1.7.1.1
UniProt
brenda
isoform Nia2, cf. EC 1.7.1.1
SwissProt
brenda
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brenda
NirD polypeptide
UniProt
brenda
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-
brenda
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brenda
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-
brenda
-
brenda
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metabolism
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the enzyme is necessary for nitrate/nitrite assimilation but also either detoxify nitrite or carries out fermentative ammonification in support of anaerobic catabolism. The enzyme confers a significant benefit during fermentative growth that reflects fermentative ammonification rather than detoxification. Fermentative ammonification by the enzyme allows for the energetically favorable fermentation of glucose to formate and acetate
physiological function
isoform NIA1 is the more efficient nitrite reductase while isoform NIA2 exhibits higher nitrate reductase activity
physiological function
isoform NIA1 is the more efficient nitrite reductase while isoform NIA2 exhibits higher nitrate reductase activity, reaction of EC 1.7.1.1
physiological function
-
the enzyme is a key contributor to regulation of the nitric oxide level during nitrate respiration
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12000
x * 12000, NirD polypeptide, SDS-PAGE
86600
x * 86600, calculated from amino acid sequence
88000
-
x * 88000, SDS-PAGE
88000
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2 * 88000, SDS-PAGE
88000
-
x * 88000, apoprotein, SDS-PAGE
90000
x * 90000, His6-tagged enzyme, SDS-PAGE
90000
x * 90000, NirB polypeptide, SDS-PAGE
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homodimer
-
2 * 88000, SDS-PAGE
?
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x * 88000, SDS-PAGE
?
x * 12000, NirD polypeptide, SDS-PAGE
?
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x * 88000, apoprotein, SDS-PAGE
?
x * 90000, NirB polypeptide, SDS-PAGE
?
A0A8D4BLJ9; A0A8D4BRF4
x * 87336, electron transfer subunit, x * 80100 catalytic subunit, SDS-PAGE
?
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x * 87336, electron transfer subunit, x * 80100 catalytic subunit, 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
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?
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x * 90000, His6-tagged enzyme, SDS-PAGE
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heterodimer
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1 * 100000 + 1 * 14000, SDS-PAGE
heterodimer
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1 * 91750 + 1 * 12400, calculated from amino acid sequence
heterodimer
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1 * 100000 + 1 * 14000, SDS-PAGE
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heterodimer
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1 * 91750 + 1 * 12400, calculated from amino acid sequence
-
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additional information
expression of the N-terminal fragment of NIA1, residues 1-627, i.e. NIA1-Mo-heme
additional information
expression of the N-terminal fragment of NIA1, residues 1-627, i.e. NIA1-Mo-heme
additional information
expression of the N-terminal fragment of NIA2, residues 1-625, i.e. NIA2-Mo-heme
additional information
expression of the N-terminal fragment of NIA2, residues 1-625, i.e. NIA2-Mo-heme
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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 BL21(DE3) cells
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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
expression in Escherichia coli
A0A8D4BLJ9; A0A8D4BRF4
recombinant expression as two separate fragments in Escherichia coli, the N-terminal Nia1-Mo-heme fragment and a C-terminal fragment containing hinge 2 and the FAD-domain, residues 628-917
recombinant expression as two separate fragments in Escherichia coli, the N-terminal Nia2-Mo-heme fragment and a C-terminal fragment containing hinge 2 and the FAD-domain, residues 626-917
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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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recombinant expression of the N-terminal Nia1-Mo-heme fragment and a C-terminal fragment containing hinge 2 and the FAD-domain, residues 628-917 and mixing of the fragments to restore the electron transfer path
recombinant expression of the N-terminal Nia2-Mo-heme fragment and a C-terminal fragment containing hinge 2 and the FAD-domain, residues 626-917 and mixing of the fragments to restore the electron transfer path
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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.
200
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 (P0A9I8), Escherichia coli
brenda
Wang, X.; Tamiev, D.; Alagurajan, J.; DiSpirito, A.A.; Phillips, G.J.; Hargrove, M.S.
The role of the NADH-dependent nitrite reductase, Nir, from Escherichia coli in fermentative ammonification
Arch. Microbiol.
201
519-530
2019
Escherichia coli
brenda
Song, Q.; Wang, B.; Zhao, F.; Han, Y.; Zhou, Z.
Expression, characterization and molecular docking of the assimilatory NADH-nitrite reductase from Acidovorax wautersii QZ-4
Biochem. Eng. J.
159
107589
2020
Acidovorax wautersii, Acidovorax wautersii QZ-4
-
brenda
Chu, S.; Zhang, D.; Wang, D.; Zhi, Y.; Zhou, P.
Heterologous expression and biochemical characterization of assimilatory nitrate and nitrite reductase reveals adaption and potential of Bacillus megaterium NCT-2 in secondary salinization soil
Int. J. Biol. Macromol.
101
1019-1028
2017
Priestia megaterium (A0A8D4BLJ9 and A0A8D4BRF4), Priestia megaterium WSH-002 (A0A8D4BLJ9 and A0A8D4BRF4)
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Bulot, S.; Audebert, S.; Pieulle, L.; Seduk, F.; Baudelet, E.; Espinosa, L.; Pizay, M.C.; Camoin, L.; Magalon, A.
Clustering as a means to control nitrate respiration efficiency and toxicity in Escherichia coli
mBio
10
e01832-19
2019
Escherichia coli
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Mohn, M.A.; Thaqi, B.; Fischer-Schrader, K.
Isoform-specific NO synthesis by Arabidopsis thaliana nitrate reductase
Plants (Basel)
8
67
2019
Arabidopsis thaliana (P11035), Arabidopsis thaliana (P11832)
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