1.7.1.1: nitrate reductase (NADH)
This is an abbreviated version!
For detailed information about nitrate reductase (NADH), go to the full flat file.
Word Map on EC 1.7.1.1
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1.7.1.1
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seedling
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molybdenum
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chlorophyll
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shoot
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biomass
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reductases
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denitrification
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ammonia
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neurospora
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denitrify
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maize
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chlorate
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alga
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tungstate
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crassa
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chlorella
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nidulans
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barley
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fumarate
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xanthine
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spinach
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urease
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nitrogenase
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dissimilatory
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viologen
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stomatal
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molybdate
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molybdoenzymes
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hydroponic
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chlamydomonas
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foliar
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molybdopterin
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gogat
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napa
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n2o
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nitrous
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isoniazid
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denitrificans
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paracoccus
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griess
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kno3
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mycorrhizal
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transpiration
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plumbaginifolia
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tungsten
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anammox
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ethambutol
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sausage
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6.3.1.2
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dinitrogen
- 1.7.1.1
- seedling
- molybdenum
- chlorophyll
- shoot
- biomass
- reductases
-
denitrification
- ammonia
- neurospora
-
denitrify
- maize
- chlorate
- alga
- tungstate
- crassa
- chlorella
- nidulans
- barley
- fumarate
- xanthine
- spinach
- urease
- nitrogenase
-
dissimilatory
- viologen
-
stomatal
- molybdate
-
molybdoenzymes
-
hydroponic
- chlamydomonas
-
foliar
- molybdopterin
- gogat
-
napa
- n2o
-
nitrous
- isoniazid
- denitrificans
- paracoccus
-
griess
- kno3
- mycorrhizal
-
transpiration
- plumbaginifolia
- tungsten
-
anammox
- ethambutol
-
sausage
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6.3.1.2
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dinitrogen
Reaction
Synonyms
assimilatory NADH:nitrate reductase, Assimilatory nitrate reductase, cytosolic NADH nitrate reductase, EC 1.6.6.1, EC 1.7.99.4, MSMEG_4206, MSMEI_4108, NADH-dependent nitrate reductase, NADH-Nar, NADH-nitrate reductase, NADH-NO3- reductase, NADH:nitrate oxidoreductase, NaR, NaR1, NasA, NasC, NIA1, Nia2, nitrate reductase, NR, NR1, NR2, Pden_4449, reductase, nitrate
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General Information
General Information on EC 1.7.1.1 - nitrate reductase (NADH)
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evolution
metabolism
physiological function
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the enzyme contains a cysteine ligand and two oxido-ligands, and is a member of the sulfite oxidase, SO, family, defined by the identity of the ligands bound to the Mo center
evolution
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the enzyme contains a cysteine ligand and two oxido-ligands, and is a member of the sulfite oxidase, SO, family, defined by the identity of the ligands bound to the Mo center
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nitric oxide is an important signaling molecule regulating nitrate reductase activity, and cGMP participates as secondary messenger on this regulation by phosphorylation and desphosphorylation processes
metabolism
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the reductive NO production pathway uses nitrite as substrate for NO production and involves either the nitrate reductase enzyme, the plasma membrane-bound nitrite:NO reductase, or mitochondrial nitrite reduction
metabolism
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the reductive NO production pathway uses nitrite as substrate for NO production and involves either the nitrate reductase enzyme, the plasma membrane-bound nitrite:NO reductase, or mitochondrial nitrite reduction. Plant nitrate reductase-dependent mARC activity, NOFNiR, can catalyze NO production from nitrite in the presence of millimolar concentrations of nitrate, which strongly inhibits the NO producing nitrite reductase activity of the nitrate reductase. Two molybdoenzymes, nitrate reductase NR and nitrate reductase-dependent mARC, are needed together for NO production in plants. The dual system NR and mARC is the major player for NO production in plants. This cytosolic NO synthesis is strictly dependent on the nitrate reductase-diaphorase activity, and independent of the Moco domain of nitrate reductase
metabolism
NarJ serves as a chaperone for both the anaerobic respiratory nitrate reductase (NarG, cf. EC 1.7.5.1) and the assimilatory nitrate reductase NasC, the latter of which is active during both aerobic and anaerobic nitrate assimilation. Both NasC and NarG are inactive in the absence of NarJ. 50% of NarJ binds in a 1:1 complex with NasC and the remaining 50% binds in a 1:1 complex with NarG
metabolism
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NarJ serves as a chaperone for both the anaerobic respiratory nitrate reductase (NarG, cf. EC 1.7.5.1) and the assimilatory nitrate reductase NasC, the latter of which is active during both aerobic and anaerobic nitrate assimilation. Both NasC and NarG are inactive in the absence of NarJ. 50% of NarJ binds in a 1:1 complex with NasC and the remaining 50% binds in a 1:1 complex with NarG
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nitrate reductase is the first enzyme in the nitrogen assimilatory pathway, which reduces nitrate to nitrite. Nitrate reductase is a key enzyme in nitrogen metabolism, that has been implicated in the production of nitric oxide (NO) in plants. In the red macroalga, nitrate reductase activity is modulated by photosynthetic electron transport chain and nitric oxide balance, direct dependence of nitrate reductase activity on the PSII and PSI electron flux, overview
physiological function
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the enzyme, instead of cytochrome b5 components, provides the electrons required for the reduction of nitrite to NO by amidoxime reducing component, i.e. crARC, or NO forming nitrite reductase, i.e. NOFNiR, respectively. Eukaryotic nitrate reductase is a cytoplasmic enzyme that catalyzes the reduction of nitrate to nitrite, which is the first step of nitrate assimilation in plants, algae and fungi. To synthesize NO from nitrite, nitrate reductase is able to substitute Cytb5 and Cytb5-R by mARC as acceptors of the electrons coming from NAD(P)H. NItrate reductase is playing a central role in plant biology by modulating the levels of NO
physiological function
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the enzyme, instead of cytochrome b5 components, provides the electrons required for the reduction of nitrite to NO by mitochondrial amidoxime reducing component, i.e. mARC, or NO forming nitrite reductase, i.e. NOFNiR, respectively. Eukaryotic nitrate reductase is a cytoplasmic enzyme that catalyzes the reduction of nitrate to nitrite, which is the first step of nitrate assimilation in plants, algae and fungi
physiological function
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a nitrate reductase-deficient mutant is capable of reducing nitrate at a rate sufficient to support growth rates approaching that of the control. The overall fate of the absorbed nitrate is basically similar between the two genotypes under light/dark cycle. Nitrate reduction in the mutant shoots is 9% lower than that in the control shoots at 38 h. Nitrate accumulation in mutant shoots is 78% higher than that in the control. Accumulation of reduced 15N in the mutant roots is 8% lower in the mutant shoots than in the control shoots at the end of the experiment
physiological function
a total of 74 genes are induced in cells grown with nitrate as N-source compared with ammonium, including nasTSABGHC and ntrBC genes. The nasABGHC genes constitute a transcriptional unit. The nasTS and nasABGHC transcripts are detected at similar levels with nitrate or glutamate as N-source, but nasABGHC transcript is undetectable in ammonium-grown cells. The nasT mutant lacks both nasABGHC transcript and nicotinamide adenine dinucleotide (NADH)-dependent nitrate reductase activity. The nasS mutant shows similar levels of the nasABGHC transcript to the wild-type strain and displays NasG protein and NADH-nitrate reductase activity with all N-sources tested, except with ammonium
physiological function
isoform NIA1 is the more efficient nitrite reductase while isoform NIA2 exhibits higher nitrate reductase activity
physiological function
NarB, NarGHJI, dehydrogenase MSMEG_2237 and MSMEG_6816 are not required for nitrate reduction as MSMEG_4206 serves as the sole assimilatory nitrate reductase
physiological function
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a total of 74 genes are induced in cells grown with nitrate as N-source compared with ammonium, including nasTSABGHC and ntrBC genes. The nasABGHC genes constitute a transcriptional unit. The nasTS and nasABGHC transcripts are detected at similar levels with nitrate or glutamate as N-source, but nasABGHC transcript is undetectable in ammonium-grown cells. The nasT mutant lacks both nasABGHC transcript and nicotinamide adenine dinucleotide (NADH)-dependent nitrate reductase activity. The nasS mutant shows similar levels of the nasABGHC transcript to the wild-type strain and displays NasG protein and NADH-nitrate reductase activity with all N-sources tested, except with ammonium
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physiological function
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NarB, NarGHJI, dehydrogenase MSMEG_2237 and MSMEG_6816 are not required for nitrate reduction as MSMEG_4206 serves as the sole assimilatory nitrate reductase
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