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Information on EC 1.7.1.1 - nitrate reductase (NADH) and Organism(s) Arabidopsis thaliana and UniProt Accession P11035
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1.7.1.1 nitrate reductase (NADH)IUBMB Comments
An iron-sulfur molybdenum flavoprotein.
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Word Map
- 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
-
6.3.1.2
-
dinitrogen
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nitrate reductase, nadh-nitrate reductase, nadh-dependent nitrate reductase, assimilatory nadh:nitrate reductase, nadh-nar, msmeg_4206, nadh:nitrate oxidoreductase, nitrate reductase (nadh), nadh-no3- reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
assimilatory NADH:nitrate reductase
-
-
-
-
Assimilatory nitrate reductase
-
-
-
-
NADH-dependent nitrate reductase
-
-
-
-
NADH-nitrate reductase
-
-
-
-
NADH:nitrate oxidoreductase
-
-
-
-
NR1
-
-
-
-
NR2
-
-
-
-
reductase, nitrate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nitrite + NAD+ + H2O = nitrate + NADH + H+
catalytic rate is determined by a combination of rates with no overall rate limiting individual process
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nitrite:NAD+ oxidoreductase
An iron-sulfur molybdenum flavoprotein.
CAS REGISTRY NUMBER
COMMENTARY
9013-03-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
?
additional information
?
-
enzyme additionally reduces nitrite, reaction of EC 1.7.1.15
-
-
-
additional information
?
-
enzyme additionally reduces nitrite, reaction of EC 1.7.1.15
-
-
-
additional information
?
-
-
enzyme additionally reduces nitrite, reaction of EC 1.7.1.15
-
-
-
additional information
?
-
enzyme additionally reduces nitrite, reaction of EC 1.7.1.15
-
-
-
additional information
?
-
enzyme additionally reduces nitrite, reaction of EC 1.7.1.15
-
-
-
additional information
?
-
-
enzyme additionally reduces nitrite, reaction of EC 1.7.1.15
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14-3-3 protein isoform chi
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform epsilon
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform kappa
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform lambda
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform ni
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform omega
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform phi
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
14-3-3 protein isoform theta
-
noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
Co-cultivation of Arabidopsis seedlings with Piriformospora indica causes a 29.8% increase in the plant-specific NADH-dependent NR activity in the roots
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
nitrate
N-terminal plus C-terminal fragment, pH 7, 22°C
0.017
nitrate
N-terminal plus C-terminal fragment, pH 7, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.4
nitrate
N-terminal plus C-terminal fragment, pH 7, 22°C
9.6
nitrate
N-terminal plus C-terminal fragment, pH 7, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00034
14-3-3 protein isoform chi
-
22°C, pH not specified in the publication
-
0.00014
14-3-3 protein isoform kappa
-
22°C, pH not specified in the publication
-
0.00008
14-3-3 protein isoform lambda
-
22°C, pH not specified in the publication
-
0.00023
14-3-3 protein isoform ni
-
22°C, pH not specified in the publication
-
0.00006
14-3-3 protein isoform omega
-
22°C, pH not specified in the publication
-
0.00031
14-3-3 protein isoform phi
-
22°C, pH not specified in the publication
-
0.00076
14-3-3 protein isoform theta
-
22°C, pH not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
guard cell, generating nitric oxide in response to treatment with abscisic acid and nitrite
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NIA2_ARATH
917
0
102844
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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 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 NIA1, residues 1-627, i.e. NIA1-Mo-heme
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Glycerol
enzyme activity is strongly negatively impacted by increase in solution viscosity using 50% glycerol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Skipper, L.; Campbell, W.H.; Mertens, J.A.; Lowe, D.J.
Pre-steady-state kinetic analysis of recombinant Arabidopsis NADH:nitrate reductase. Rate-limiting processes in catalysis
J. Biol. Chem.
276
26995-27002
2001
Arabidopsis thaliana
Su, W.; Mertens, J.A.; Kanamaru, K.; Campbell, W.H.; Crawford, N.M.
Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris
Plant Physiol.
115
1135-1143
1997
Arabidopsis thaliana
Desikan, R.; Griffiths, R.; Hancock, J.; Neill, S.
A new role for an old enzyme: nitrate reductase-mediated nitric oxide generation is required for abscisic acid-induced stomatal closure in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
99
16314-16318
2002
Arabidopsis thaliana
Sherameti, I.; Shahollari, B.; Venus, Y.; Altschmied, L.; Varma, A.; Oelmueller, R.
The endophytic fungus Piriformospora indica stimulates the expression of nitrate reductase and the starch-degrading enzyme glucan-water dikinase in tobacco and Arabidopsis roots through a homeodomain transcription factor that binds to a conserved motif in their promoters
J. Biol. Chem.
280
26241-26247
2005
Arabidopsis thaliana, Nicotiana tabacum
Barbier, G.G.; Campbell, W.H.
Viscosity effects on eukaryotic nitrate reductase activity
J. Biol. Chem.
280
26049-26054
2005
Arabidopsis thaliana (P11035), Zea mays (Q9XGW5)
Lambeck, I.; Chi, J.C.; Krizowski, S.; Mueller, S.; Mehlmer, N.; Teige, M.; Fischer, K.; Schwarz, G.
Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase
Biochemistry
49
8177-8186
2010
Arabidopsis thaliana
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