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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 1 Oxidoreductases
1.7 Acting on other nitrogenous compounds as donors
1.7.1 With NAD+ or NADP+ as acceptor
1.7.1.15 nitrite reductase (NADH)
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
showSynonyms
nadh-dependent nitrite reductase, nirbd, nadh-nitrite reductase, nasde, assimilatory nadh-nitrite reductase, nadh-dependent nitrite oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
assimilatory NADH-nitrite reductase
assimilatory nitrite reductase
-
-
ambiguous
-
BMWSH_4089
NADH-dependent nitrite reductase
NADH-nitrite oxidoreductase
NasB
NasB protein
nasD
NasDE
nasE
nirB
NirBD
nirD
nitrite reductase (reduced nicotinamide adenine dinucleotide)
-
-
-
-
NADH-dependent nitrite reductase
-
-
NADH-nitrite oxidoreductase
-
-
-
-
nirB
-
-
-
-
nirD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NH3 + 3 NAD+ + 2 H2O = nitrite + 3 NADH + 5 H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
Substrates: -
Products: -
Products: -
?
ferricytochrome c + NADH + H+
ferrocytochrome c + NAD+
-
Substrates: -
Products: -
Products: -
r
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
Acidovorax wautersii QZ-4
-
Substrates: -
Products: -
Products: -
?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
Substrates: NADH is the best acceptor
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
Substrates: NADH is the best acceptor
Products: -
Products: -
?
nitrite + NADH + H+
nitrite + NAD+ + H2O
A0A8D4BLJ9; A0A8D4BRF4
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
nitrite + NAD+ + H2O
A0A8D4BLJ9; A0A8D4BRF4
Substrates: -
Products: -
Products: -
?
nitrite + reduced benzyl viologen
ammonia + oxidized benzyl viologen
Substrates: -
Products: -
Products: -
?
nitrite + reduced benzyl viologen
ammonia + oxidized benzyl viologen
Substrates: -
Products: -
Products: -
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
Substrates: -
Products: -
Products: -
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
-
Substrates: -
Products: -
Products: -
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
A0A8D4BLJ9; A0A8D4BRF4
Substrates: the optimum electron donor is methyl viologen plus Na2S2O4
Products: -
Products: -
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
A0A8D4BLJ9; A0A8D4BRF4
Substrates: the optimum electron donor is methyl viologen plus Na2S2O4
Products: -
Products: -
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
Substrates: -
Products: -
Products: -
?
nitrite + reduced methyl viologen
ammonia + oxidized methyl viologen
Substrates: -
Products: -
Products: -
?
nitrite + reduced methyl viologen
NH3 + oxidized methyl viologen
-
Substrates: methyl viologen is the best in vitro electron donor
Products: -
Products: -
?
nitrite + reduced methyl viologen
NH3 + oxidized methyl viologen
Acidovorax wautersii QZ-4
-
Substrates: methyl viologen is the best in vitro electron donor
Products: -
Products: -
?
additional information
?
-
Substrates: NirB, NirD polypeptides are essential for NADH-dependent nitrite reductase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: NirB, NirD polypeptides are essential for NADH-dependent nitrite reductase activity
Products: -
Products: -
?
additional information
?
-
Substrates: NADPH is not an effcient electron donor
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADPH is not an effcient electron donor
Products: -
Products: -
?
additional information
?
-
Substrates: NADPH is not an effcient electron donor
Products: -
Products: -
?
additional information
?
-
-
Substrates: NADPH is not an effcient electron donor
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
Acidovorax wautersii QZ-4
-
Substrates: -
Products: -
Products: -
?
nitrite + 3 NADH + 5 H+
NH3 + 3 NAD+ + 2 H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
Substrates: NADH is the best acceptor
Products: -
Products: -
?
nitrite + NADH + H+
ammonia + NAD+ + H2O
Substrates: NADH is the best acceptor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
-
the enzyme contains 5 Fe atoms and 4 acid-labile S atoms per subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
additional information
-
Mg2+ and Mn2+ have no evident effects on enzyme activity
additional information
A0A8D4BLJ9; A0A8D4BRF4
not inhibitory nor activating: Ba2+, EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCN
-
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+
-
NAD+ shows mixed product inhibition with respect to NADH and mixed or uncompetitive inhibition with respect to hydroxylamine
nitrite
-
nitrite decrease the rate of NADH-dependent reduction of cytochrome c by 77% and that of Fe(CN)63- by 90%
p-chloromercuribenzoate
-
the reduction of cytochrome c, K3Fe(CN)6 and hydroxylamine is completely inhibited (more than 99%) by 0.02 mM p-chloromercuribenzoate
additional information
-
dithiothreitol and EDTA have no evident effects on enzyme activity
-
additional information
A0A8D4BLJ9; A0A8D4BRF4
not inhibitory nor activating: Ba2+, EDTA
-
additional information
the activity of the His6-tagged NasB protein is unaffected by thiocyanate
-
additional information
-
the activity of the His6-tagged NasB protein is unaffected by thiocyanate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
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+
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0488
NADH
-
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
0.0353
nitrite
N-terminal plus C-terminal fragment, pH 7.5, 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
nitrite
N-terminal plus C-terminal fragment, pH 7, 22°C
137.5
nitrite
N-terminal plus C-terminal fragment, pH 7.5, 22°C
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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
5 - 7
-
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30
-
over 93% activity is retained at 40°C. At 20 and 50°C, the enzyme retains more than 73 and 66% activity, respectively
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
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
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
Show AA Sequence and Transmembrane Helices (1941 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
88000
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
?
A0A8D4BLJ9; A0A8D4BRF4
x * 87336, electron transfer subunit, x * 80100 catalytic subunit, SDS-PAGE
?
-
x * 87336, electron transfer subunit, x * 80100 catalytic subunit, SDS-PAGE
-
heterodimer
-
1 * 91750 + 1 * 12400, calculated from amino acid sequence
heterodimer
Acidovorax wautersii QZ-4
-
1 * 91750 + 1 * 12400, calculated from amino acid sequence
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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