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
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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
ECTree
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Engineering
Engineering on EC 1.7.1.1 - nitrate reductase (NADH)
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S521D
C17S
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visible and CD spectra are very similar to that of the wild-type domain, thermal stability is slightly decreased compared to the wild-type domain
C240S
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decrease of diaphorase activity, thermal stability is slightly decreased compared to the wild-type domain, the oxidation reduction midpoint potential for the FAD/FADH2 couple is -219 mV compared to -268 mV in the wild-type domain
C54S
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visible and CD spectra are very similar to that of the wild-type domain, thermal stability is slightly decreased compared to the wild-type domain,the oxidation reduction midpoint potential for the FAD/FADH2 couple is -197 mV compared to -268 mV in the wild-type domain
C62S
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visible and CD spectra are very similar to that of the wild-type domain, thermal stability is decreased compared to the wild-type domain, the oxidation reduction midpoint potential for the FAD/FADH2 couple is -226 mV compared to -268 mV in the wild-type domain
K714A
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
K741E
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
K741H
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
K741M
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
K741P
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
K741Q
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
K741R
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functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order
additional information
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complete abolishment of inactivation in response to light/dark transition rendering enzyme in activated form. Upon high nitrate concentrations, transgenic plants accumulate nitrite in darkness and young leaves show chlorosis
S521D
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the protein is constitutively active under conditions where the wild type protein would be rapidly inactivated, such as in the dark
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
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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
additional information
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expression of the N-terminal fragment of NIA2, residues 1-625, i.e. NIA2-Mo-heme
additional information
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ammonia levels in the wild-type are decreased by about one-half by CO2 enrichment, whereas ammonia is unaffected by elevated CO2 in nar1 mutant leaves
additional information
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expression of 541 residue amonio-terminal, molybdenum-containing domain in Escherichia coli either as His-tagged or GST-tagged fusion protein
additional information
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expression of fragment A542-Y647 in Escherichia coli, production of enzyme heme domain evidenced by pink cells. Reconstitution of NADH:cytochrome c reductase activity in presence of recombinant form of spinach nitrate reductase flavin domain