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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
benzoquinone + NADH
benzoquinol + NAD+
-
-
-
-
?
bromophenol blue + nitrate
? + nitrite
Cucurbita sp.
-
-
-
-
?
FADH2 + nitrate
FAD + nitrite
flavin hydroquinone + nitrate
? + nitrite
-
-
-
-
?
FMNH2 + nitrate
FMN + nitrite
menadione + NADH
reduced menadione + NAD+
-
-
-
-
?
methylene blue + NADH
reduced methylene blue + NAD+
-
-
-
-
?
NADH + BrO3-
NAD+ + ?
-
-
-
-
?
NADH + ClO3-
NAD+ + ?
-
-
-
-
?
NADH + IO3-
NAD+ + ?
-
-
-
-
?
NADH + nitrate + H+
NAD+ + H2O + nitrite
-
-
-
-
?
NADH + nitrate + H+
NAD+ + nitrite + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
nitrate + NADH + H+
nitrite + NAD+
nitrate + NADH + H+
nitrite + NAD+ + H2O
nitrate + NADPH
nitrite + NADP+ + H2O
nitrite + NADH
nitric oxide + NAD+ + H2O
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
reduced bromophenol blue + nitrate
bromophenol blue + nitrite
reduced flavin + nitrate
? + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
additional information
?
-
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
FADH2 + nitrate
FAD + nitrite
-
-
-
-
?
FADH2 + nitrate
FAD + nitrite
-
-
-
-
?
FADH2 + nitrate
FAD + nitrite
-
-
-
-
?
FADH2 + nitrate
FAD + nitrite
-
-
-
-
?
FMNH2 + nitrate
FMN + nitrite
-
-
-
-
?
FMNH2 + nitrate
FMN + nitrite
-
-
-
-
?
FMNH2 + nitrate
FMN + nitrite
-
-
-
-
?
FMNH2 + nitrate
FMN + nitrite
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
Ankistrodesmus braunii
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
Cucurbita sp.
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
Pisum arvense
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
392837, 392843, 392852, 392853, 392859, 392862, 392870, 392871, 392872, 392880, 392882, 392884, 392886, 392891, 392897, 392899, 392902, 392903, 392915, 392916, 392917 -
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
the enzyme catalyzes the regulated and rate-limiting step in the utilization of inorganic nitrogen by higher plants
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
ir
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
287994, 392845, 392855, 392865, 392869, 392876, 392878, 392883, 392886, 392891, 392893, 392894, 392900 -
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
?
nitrate + NADH
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH + H+
nitrite + NAD+
-
-
-
-
r
nitrate + NADH + H+
nitrite + NAD+
-
-
-
-
r
nitrate + NADH + H+
nitrite + NAD+
-
-
-
-
r
nitrate + NADH + H+
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADH + H+
nitrite + NAD+ + H2O
the enzyme is involved in the reduction of NO3- to nitrite at the initial step of denitrification
-
-
?
nitrate + NADH + H+
nitrite + NAD+ + H2O
the enzyme is involved in the reduction of NO3- to nitrite at the initial step of denitrification
-
-
?
nitrate + NADH + H+
nitrite + NAD+ + H2O
-
-
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
no activity
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
much more active with NADH
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
no activity
-
-
?
nitrate + NADPH
nitrite + NADP+ + H2O
-
no activity
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH
? + NAD+
-
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
reduced bromophenol blue + nitrate
bromophenol blue + nitrite
-
-
-
-
?
reduced bromophenol blue + nitrate
bromophenol blue + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
-
-
-
-
?
additional information
?
-
-
in extracts of algae grown under either constant dimlight or light-dark cycle, the activity of nitrate reductase exhibits a daily rhythm, peaking at midday phase as does photosynthesis
-
-
?
additional information
?
-
-
induction by nitrate and cytokinin
-
-
?
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
?
-
-
constitutive nitrate reductase
-
-
?
additional information
?
-
-
constitutive nitrate reductase
-
-
?
additional information
?
-
-
the nitrate reductase interacts with the crARC in Chlamydomonas reinhardtii
-
-
?
additional information
?
-
-
partial activities reside on functionally independent domains
-
-
?
additional information
?
-
-
the enzyme could have a role in iron assimilation
-
-
?
additional information
?
-
-
no activity with coenzyme Q10 and plastoquinone
-
-
?
additional information
?
-
-
key enzyme of nitrogen metabolism in higher plants
-
-
?
additional information
?
-
-
minor role of enzyme in the regulation of nitrate assimilation pathway
-
-
?
additional information
?
-
-
effect of nitrate, ammonium, light and a plastidic factor on the appearance of multiple forms of nitrate reductase
-
-
?
additional information
?
-
-
the isolated flavin-containing domain is capable of reducing cytochrome b5 directly
-
-
?
additional information
?
-
-
NADH-diaphorase activity
-
-
?
additional information
?
-
-
NADH-diaphorase activity
-
-
?
additional information
?
-
-
induced by nitrate
-
-
?
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14-3-3 protein BMH1
-
0.0018 mM, reduces activity to less than 20%, at pH 6.0
-
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
-
2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
a photosynthetic electron flux inhibitor of photosystem I, causes 61% inhibition at 0.008 mM
2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid
2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide
-
a NO scavenger
3-(3,4-dichlorophenyl)-1,1-dimethylurea
adenine
-
inhibition of the recombinant FAD domain
adenosine
-
inhibition of the recombinant FAD domain
adenosine 5'-diphosphoribose
AMP
-
inhibition of the recombinant FAD domain
ATP
-
at low pH, the presence of ATP alone in the incubation medium is sufficient to inactivate nitrate reductase
Bromophenol blue
Cucurbita sp.
-
noncompetitive versus NADH
Ca2+
-
5 mM, 90% inhibition of the low activity form, no activity of high activity form, inhibition is prevented by low concentrations of thiol compounds
Carbamoyl phosphate
-
competitive
Cd2+
-
0.002 mM, 40% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration
Cl-
-
alters the observed Mo(V) lineshape, mixed-type inhibitor, decreases both NADH:nitrate reductase and reduced methyl viologen:nitrate reductase activities
Co2+
-
1 mM, strong inhibition
Cr
-
after 24 h activity is reduced by 17.31%, 30.72% and 45% at 1 mM, 10 mM and 100 mM of Cr, respectively
Cr3+
-
0.002 mM, 20% inhibition, 10 mM nitrilotriacetic acid does not protect
Cr6+
-
0.001 mM, 62% inhibition, 10 mM nitrilotriacetic acid does not protect
Cu
-
after 24 h activity is reduced by 21.5%, 36% and 46% at 1 mM, 10 mM and 100 mM of Cu, respectively
dicoumarol
-
competitive towards NADH
dithiothreitol
-
rate of inactivation is increased by NAD+, but not by NADP+
Fe2+
-
potent inhibitor, inhibition can be abolished by prior chelation of the metal by EDTA
Fe3+
-
less potent inhibitor, effect cannot reversed by EDTA
ferricyanide
-
inhibition of the recombinant FAD domain
ferrocytochrome c
-
inactivation in a biphasic reaction, immune to inactivation during turnover with nitrate
glutamine
-
1 mM, decrease of activity
KCN
-
0.1 mM, complete inhibition
menadione
-
inhibits nitrate reductase
methyl methanethiosulfonate
MoO42-
-
1 mM, strong inhibition
mutant G216S of 14-3-3A protein
-
-
-
N-ethylmaleimide
-
1 mM, complete inhibition
NaN3
-
0.1 mM, complete inhibition
Ni2+
-
up to 0.1 mM, not inhibitory, 1 mM, 20% residual activity
nicotinamide
-
inhibition of the recombinant FAD domain
NMN
-
inhibition of the recombinant FAD domain
NO2-
-
10 mM, 65% inhibition
o-phenanthroline
-
1 mM, complete inhibition
p-chloromercuribenzoic acid
-
0.01 mM, complete inhibition
phosphate
-
25 mM, increases activity with a nitrate concentration of 2 mM, decreases activity with a nitrate concentration of 0.1 mM
potassium ferricyanide
-
preincubation with potassium ferricyanide inactivates nitrate reductase
sodium nitroprusside
-
a NO donor
VO3-
-
1 mM, strong inhibition
Zn
-
after 24 h activity is reduced by 11%, 19% and 21% at 1 mM, 10 mM and 100 mM of Cr, respectively
2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid
-
-
2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid
-
-
3-(3,4-dichlorophenyl)-1,1-dimethylurea
-
a photosynthetic electron flux inhibitor of photosystem II, causes 51% inhibition at 0.001 mM
3-(3,4-dichlorophenyl)-1,1-dimethylurea
-
inhibits the post-translational light activation of nitrate reducate
adenosine 5'-diphosphoribose
-
dead-end inhibition
adenosine 5'-diphosphoribose
-
inhibition of the recombinant FAD domain
ADP
-
competitive with ADP
ADP
-
inhibition of the recombinant FAD domain
azide
-
1 mM sodium azide, 90% inhibition of nitrate reduction; sodium azide
azide
-
inhibition of full and nitrate-reducing partial activities
Cu2+
-
0.001 mM, 76% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration
Cu2+
-
potent inhibitor, inhibition can be abolished by prior chelation of the metal by EDTA
Cu2+
-
1 mM, strong inhibition
cyanide
-
-
cyanide
-
potent inhibitor
cyanide
-
inhibition of full and nitrate-reducing partial activities
cyanide
-
potent inhibitor
cyanide
-
mechanism of reactivation of cyanide-inactivated nitrate reductase by flavins in light
cyanide
-
reactivation by incubation with oxidant systems after inactivation by treatment with NADH and cyanide
cyanide
-
inactivation by simultaneous presence of NADH and low concentrations of cyanide, reactivation by incubation with ferricyanide or by a short exposure to light in the presence of FAD
hydroxylamine
Ankistrodesmus braunii
-
NO3-, cyanate, carbamoyl phosphate and azide protect from inactivation. Photoreactivation in presence of flavins, early inhibition appears to be competitive versus NO3-
hydroxylamine
-
interacts with reduced cytochrome b557 during catalysis of the enzyme
methyl methanethiosulfonate
-
-
methyl methanethiosulfonate
-
inactivation is concentration independent
Mg2+
-
5 mM MgCl2 decreases enzyme activity at pH 7.5, this effect is completely reversed by the addition of EDTA into samples returning the enzyme's activity to its initial level
Mg2+
-
5 mM, 70% inhibition of the low activity form, no inhibition of high activity form, inhibition is prevented by low concentrations of thiol compounds
Mg2+
native protein, highly sensitive to Mg2+, recombinant protein, not sensitive. Recombinant protein plus enzyme-free leaf extract of Ricinus communis shows restored high sensitivity to Mg2+, but remains unresponsive to ATP
MgCl2
-
10 mM, 75% decrease of activity
MgCl2
-
0.1-5 mM, strong, both cytosolic and membrane-bound isozyme
Mn2+
-
less potent inhibitor, effect cannot be reversed by EDTA
Mn2+
-
1 mM, 27% inhibition
NaCl
-
100 mM
NaCl
-
uncompetitive for nitrate and NADH
NaCl
-
100 mM NaCl reduces enzyme activity in leaves from plants grown on 10 mM nitrate and in roots from plants grown on 0.1 mM nitrate to about 50%
NAD+
-
product inhibition
NAD+
-
competitive towards NADH
NAD+
-
inhibition of the recombinant FAD domain
NAD+
-
inactivation in presence of thiol compounds is enhanced by cyanide ions and can be reversed by ferricyanide
NAD+
-
competitive towards NADH
NADH
-
inactivation in a biphasic reaction, immune to inactivation during turnover with nitrate
NADH
-
p-hydroxymercuribenzoate causes the appearance of an FAD-requirement for inactivation by NADH of FMNH2-nitrate reductase
NADH
-
conversion of the enzyme to a reduced inactive form, by preincubation with NADH, in absence of nitrate, occurs in presence of either dithiothreitol and/or FAD but not with cysteine. Pretreatment with NADH alone does not inactivate, a nucleophilic agent, i.e. cyanide or superoxide is necessary to inhibit electron transfer by the enzyme to nitrate
NADH
-
0.01 mM NADH, in absence of nitrate, 50% loss of activity after 30 min, 0.05 mM nitrate prevents inactivation, 0.001 mM cyanide enhances degree of inactivation. Rapid reactivation after treatment with 0.3 mM ferricyanide or exposure to light, 230 mWatt per cm2, plus 0.02 mM flavin adenine dinucleotide
NEM
-
-
NEM
-
inhibition of full and NADH-utilizing partial activities
NH4+
-
-
nitrite
-
-
nitrite
-
product inhibition
nitrite
-
competitive towards nitrate
nitrite
-
competitive towards nitrate
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
Cucurbita sp.
-
inactivation of NADH:nitrate reductase activity, no loss of bromphenol blue: nitrate reductase activity
p-hydroxymercuribenzoate
-
inhibition of full and NADH-utilizing partial activities
p-hydroxymercuribenzoate
-
dissapearance of NADH-diaphorase activity
p-hydroxymercuribenzoate
-
-
Pb2+
-
0.002 mM, 60% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration
Pb2+
-
less potent inhibitor, effect cannot reversed by EDTA
PCMB
-
-
PCMB
-
inactivation is concentration independent
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
uncompetitive with nitrate
thiocyanate
-
-
thiocyanate
-
dead-end inhibition
Zn2+
-
0.004 mM, 60% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration
Zn2+
-
potent inhibitor, inhibition can be abolished by prior chelation of the metal by EDTA
Zn2+
-
1 mM, strong inhibition
additional information
-
no enzyme inhibition by diphenyleneiodonium, i.e. DPI, a NADPH oxidase inhibitor, and poor inhibition by L-NG-monomethyl arginine citrate (L-NMMA), a NOS inhibitor. But nitrate reductase activity is sensitive to a decrease or increase of NO levels when NO scavenger 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide and NO donor sodium nitroprusside are added
-
additional information
-
increasing level of salinity causes decrease in enzyme activity
-
additional information
-
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
-
additional information
-
An inhibitory effect of Mg-ATP is cancelled in the presence of staurosporine (the protein kinase inhibitor) and completely reversed after addition of EDTA as well as AMP
-
additional information
-
inhibition by monospecific anti-nitrate reductase rabbit serum
-
additional information
-
purification of a NADH-nitrate reductase inhibitor from young leaves of Glycine max, that causes a reversible inhibition
-
additional information
-
the 14-3-3A protein and the 14-3-3C protein are functionally not capable to inhibit nitrate reductase
-
additional information
-
the enzyme is insensitive to oxygen
-
additional information
-
not inhibitory: ammonium, glutamine
-
additional information
-
roots of seedlings from Oryza sativa contain a substance which inhibits the activity of nitrate reductase when NADH or FMNH2 is used as electron donor
-
additional information
-
inhibitor from primary and regenerated roots of nitrate-grown seedlings, main site of action is NADH:cytochrome c reductase component of the nitrate reductase, NADH protects
-
additional information
-
nitrate reductase inhibitor from root extract of rice seedlings. Inactivation proceeds in two steps: the inhibitor first binds with nitrate reductase to cause a reduction in both NADH:nitrate reductase and reduced benzyl viologen:nitrate reductase activity. In the second phase, there is a complete inactivation of NADH:nitrate reductase after about 20 min. Reduced benzyl viologen:nitrate reductase activity is not affected by the second phase of inactivation
-
additional information
Pisum arvense
-
maize root inactivating enzyme inactivates pea leaf nitrate reductase
-
additional information
-
maize root inactivating enzyme inactivates NADH:cytochrome c reductase at a greater rate than FADH2:nitrate reductase
-
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0.739
BrO3-
-
ionic strength: 50 mM
0.06
Bromophenol blue
Cucurbita sp.
-
at 10 mM nitrate
0.221
ClO3-
-
ionic strength: 50 mM
0.021 - 0.045
ferricyanide
0.006 - 80
ferricytochrome c
0.056
flavin hydroquinone
-
ionic strength: 50 mM or 200 mM
10.75
IO3-
-
ionic strength: 50 mM
0.053 - 100
oxidized 2,6-dichlorophenolindophenol
0.54
reduced bromophenol blue
-
-
-
0.87
reduced methyl viologen
-
-
additional information
additional information
-
0.021
ferricyanide
-
ionic strength: 50 mM
0.027
ferricyanide
-
wild-type recombinant flavin domain of nitrate reductase
0.034
ferricyanide
-
recombinant FAD domain
0.035
ferricyanide
-
ionic strength: 200 mM
0.036
ferricyanide
-
recombinant flavin domain of nitrate reductase C54S mutant
0.045
ferricyanide
-
recombinant flavin domain of nitrate reductase C17S mutant
0.006
ferricytochrome c
-
ionic strength: 50 mM
0.029
ferricytochrome c
-
ionic strength: 200 mM
0.0029
NADH
-
-
0.004
NADH
-
recombinant flavin domain of nitrate reductase C240A mutant
0.004
NADH
-
wild-type recombinant enzyme
0.006
NADH
-
ionic strength: 200 mM
0.007
NADH
-
ionic strength: 50 mM
0.011
NADH
-
recombinant flavin domain of nitrate reductase C240G mutant
0.012
NADH
-
wild-type recombinant flavin domain of nitrate reductase
0.014
NADH
-
recombinant flavin domain of nitrate reductase C240S mutant
0.015
NADH
-
recombinant flavin domain of nitrate reductase C17S mutant
0.015
NADH
-
recombinant flavin domain of nitrate reductase C54S mutant
0.016
NADH
-
recombinant flavin domain of nitrate reductase C62S mutant
0.017
NADH
-
recombinant FAD domain
0.024
NADH
-
recombinant flavin domain of nitrate reductase C240S mutant
0.035
NADH
-
pH 7.5, 30°C, membrane-bound isoform
0.048
NADH
-
pH 7.5, 30°C, cytosolic isoform
0.052
NADH
-
reaction with nitrate
0.059
NADH
-
recombinant flavin domain of nitrate reductase C62S mutant
0.067
NADH
-
reaction with 2,6-dichlorophenol indophenol
0.008
nitrate
-
His-tagged molybdenum domain, 25°C, pH 7.6
0.012
nitrate
-
GST-tagged molybdenum domain, 25°C, pH 7.6
0.013
nitrate
-
at ionic strength of 50 mM
0.015
nitrate
-
wild-type recombinant enzyme
0.017
nitrate
N-terminal plus C-terminal fragment, pH 7, 22°C
0.018
nitrate
-
at ionic strength of 200 mM
0.035
nitrate
N-terminal plus C-terminal fragment, pH 7, 22°C
0.09
nitrate
-
in presence of 25 mM phosphate
0.093
nitrate
-
in 5 mM phosphate buffer
0.096
nitrate
-
reaction with NADH
0.104
nitrate
-
pH 8.5, 25°C
0.13
nitrate
-
reaction with methyl viologen
0.14
nitrate
-
without phosphate
0.19
nitrate
-
reaction with NADH
0.197
nitrate
-
22°C, pH not specified in the publication
0.27
nitrate
-
pH 7.5, 30°C, cytosolic isoform
0.443
nitrate
N-terminal fragment, pH 7, 22°C
0.5
nitrate
Cucurbita sp.
-
at 0.2 mM bromophenol blue
0.97
nitrate
-
pH 7.5, 30°C, membrane-bound isoform
2.12
nitrate
N-terminal fragment, pH 7, 22°C
13
nitrate
-
reaction with bromophenol blue
0.053
oxidized 2,6-dichlorophenolindophenol
-
ionic strength: 50 mM
0.056
oxidized 2,6-dichlorophenolindophenol
-
ionic strength: 200 mM
0.13
oxidized 2,6-dichlorophenolindophenol
-
-
100
oxidized 2,6-dichlorophenolindophenol
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values of the the C-terminal 268 residues corresponding to the flavin-containing domain, amplified and expressed in E. coli
-
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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
-
0.0000015 - 0.0000017
14-3-3B protein
-
26
adenine
-
inhibition of the recombinant FAD domain
4.8
adenosine
-
inhibition of the recombinant FAD domain
0.2
ADPribose
-
inhibition of the recombinant FAD domain
0.6
AMP
-
inhibition of the recombinant FAD domain
0.3
Bromophenol blue
Cucurbita sp.
-
-
0.018
Carbamoyl phosphate
-
-
0.013
dicoumarol
-
nitrate reductase assay
23
ferricyanide
-
inhibition of the recombinant FAD domain
0.12
hydroxylamine
Ankistrodesmus braunii
-
-
0.0000049 - 0.0000054
mutant G216S of 14-3-3A protein
-
122
nicotinamide
-
inhibition of the recombinant FAD domain
62
NMN
-
inhibition of the recombinant FAD domain
0.176
pyridoxal 5'-phosphate
-
-
additional information
additional information
-
0.0000015
14-3-3B protein
-
in the presence of 5 mM Mg2+
-
0.0000017
14-3-3B protein
-
in the presence of 5 mM Ca2+
-
0.2
ADP
-
inhibition of the recombinant FAD domain
15
Cl-
-
binding to the native enzyme
176
Cl-
-
binding to the enzyme-NO3- complex
0.0000049
mutant G216S of 14-3-3A protein
-
in the presence of 5 mM Ca2+
-
0.0000054
mutant G216S of 14-3-3A protein
-
in the presence of 5 mM Mg2+
-
0.5
NAD+
-
recombinant flavin domain of nitrate reductase C240G mutant
0.8
NAD+
-
recombinant flavin domain of nitrate reductase C240A mutant
1.2
NAD+
-
recombinant flavin domain of nitrate reductase C240S mutant
1.5
NAD+
-
recombinant flavin domain of nitrate reductase C54S mutant
1.9
NAD+
-
inhibition of the recombinant FAD domain
1.9
NAD+
-
recombinant flavin domain of nitrate reductase wild-type and C17S mutant
2
NAD+
-
recombinant flavin domain of nitrate reductase C62S mutant
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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evolution
-
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
-
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
metabolism
-
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
-
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
-
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
-
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
-
physiological function
-
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
-
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
-
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
-
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
-
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
-
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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103000
-
2 * 103000, SDS-PAGE
115000
-
2 * 115000, SDS-PAGE
144000
-
non-denaturing pore gradient PAGE
180000
-
4 active fractions with MW of 91000 Da, 362000 Da, 180000 Da and 720000 Da are detected, gel filtration
20000
-
alpha2beta2gamma2molybdenum-containing-component, 2 * 40000 Da FAD-containing alpha-subunit + 2 * 20000 Da cytochrome b557 beta subunit + 2 *gamma subunit which carries molybdenum-containing component of 1000 Da
205000
-
non-denaturing PAGE
221000
-
sucrose density gradient centrifugation, gel filtration
225000
-
disc gel electrophoresis
230000
-
disc gel electrophoresis
270000
-
gel filtration, sucrose density gradient centrifugation
280000
-
equilibrium sedimentation
356000
-
sucrose density gradient centrifugation, gel filtration
360000
-
equilibrium sedimentation
362000
-
4 active fractions with MW of 91000 Da, 362000 Da, 180000 Da and 720000 Da are detected, gel filtration
40000
-
alpha2beta2gamma2molybdenum-containing-component, 2 * 40000 Da FAD-containing alpha-subunit + 2 * 20000 Da cytochrome b557 beta subunit + 2 *gamma subunit which carries molybdenum-containing component of 1000 Da
46000
-
1 * 46000 + 1 * 95000, SDS-PAGE
55000
-
x * 55000, SDS-PAGE, His-tagged domain, x * 85000, SDS-PAGE, GST-tagged domain
720000
-
4 active fractions with MW of 91000 Da, 362000 Da, 180000 Da and 720000 Da are detected, gel filtration
91000
-
4 active fractions with MW of 91000 Da, 362000 Da, 180000 Da and 720000 Da are detected, gel filtration
95000
-
1 * 46000 + 1 * 95000, SDS-PAGE
98000
-
x * 98000, SDS-PAGE
additional information
-
the C-terminal 268 residues corresponding to the flavin-containing domain, amplified and expressed in E. coli show a MW of 30000 Da by SDS-PAGE
100000
-
x * 100000, SDS-PAGE
100000
-
2 * 100000, SDS-PAGE
100000
-
2 * 100000, SDS-PAGE
100000
-
4 * 100000, at low protein concentration, the tetramer dissociates to a fully active dimer, each subunit in the tetramer or dimer can function independently, radiation inactivation analysis
110000
-
4 * 110000, SDS-PAGE
110000
-
x * 110000, SDS-PAGE
110000
-
2 * 110000, SDS-PAGE
202000
-
202000
-
sucrose density gradient centrifugation, gel filtration
85000
-
6 * 85000, SDS-PAGE
85000
-
x * 55000, SDS-PAGE, His-tagged domain, x * 85000, SDS-PAGE, GST-tagged domain
90000
-
x * 90000, equilibrium sedimentation of enzyme dissociated in 6 M guanidine hydrochloride
90000
-
4 * 90000, dihedral symmetry, SDS-PAGE
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C191A
-
enzyme is still produced, but it is inactive
C191S
-
enzyme is still produced, but it is inactive
S266A
-
48% of the activity of wild-type enzyme
S534A
-
the mutant is not inhibited by 14-3-3 proteins
C17S
-
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
C240A
-
decrease of diaphorase activity
C240G
-
decrease of diaphorase activity
C240S
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
S521D
-
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
-
the protein is constitutively active under conditions where the wild type protein would be rapidly inactivated, such as in the dark
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
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
-
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
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0.03% SDS produces almost complete inactivation of NADH-diaphorase and NADH-nitrate reductase, while FNH2-nitrate reductase retains 60% of the original activity, FAD has no protecting effect
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1 M guanidine hydrochloride, in presence of FAD, 80% inactivation of FNH2-nitrate reductase activity and NADH-nitrate reductase activity, NADH-diaphorase activity is unaffected
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4 M urea, in presence of FAD, inactivation of FMNH2-nitrate reductase and NADH-nitrate reductase activity, only a slight effect on the NADH-diaphorase activity
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dilution of a crude extract leads to increasing lability, much more stable in presence of both NADH and nitrate
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enzyme in the crude extract is stable for several days at 0°C and for several months at -80°C
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FAD protects from heat inactivation at 45°C
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FAD stabilizes at 25°C, at 10°C FAD has no effect on stability
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imposition of water stress or artificial extension of the dark period leads to significant reduction of nitrate reductase activity, but does not change in vitro nitrate reductase stability
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inactivation by corn root proteinase, comparison of hydrolysis products
incubation of the native enzyme with either trypsin, Staphylococcus aureus V8 protease, or a natural inactivator protease from corn results in loss of NADH:nitrate reductase and NADH:cytochrome c reductase activity, but no loss of methyl viologen:nitrate reductase activity
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leupeptin inhibits degradation of NADH-nitrate reductase by thiol-dependent acid endoproteinase in primary leaf extract
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preincubation with NADH stabilizes activity at 0C and at 25C
presence of casein in phosphate buffer improves stability at 0°C but not at 30°C
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stabilized at 0°C and at 30°C by buffer containing 0.25 M Tris-HCl, pH 8.5, 3 mM DTT, 0.005 mM FAD, 0.001 mM sodium molybdate and 1 mM EDTA
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stabilized in vitro by addition of chymostatin to extraction buffer
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the decay rate of nitrate reductase activity in crude extracts is due to spontaneous dissociation of the enzyme and to the effects of two decay factors, one present in the 0-30% and the other in the 50-70% saturated (NH4)2SO4 fraction of the crude extract
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the enzyme is very susceptible to inactivation by maize root proteinase and trypsin
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inactivation by corn root proteinase, comparison of hydrolysis products
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inactivation by corn root proteinase, comparison of hydrolysis products
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preincubation with NADH stabilizes activity at 0C and at 25C
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preincubation with NADH stabilizes activity at 0C and at 25C
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