1.7.1.1 14-3-3 protein BMH1 0.0018 mM, reduces activity to less than 20%, at pH 6.0 135354 1.7.1.1 14-3-3 protein isoform chi noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83949 1.7.1.1 14-3-3 protein isoform epsilon noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 163582 1.7.1.1 14-3-3 protein isoform kappa noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83955 1.7.1.1 14-3-3 protein isoform lambda noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83953 1.7.1.1 14-3-3 protein isoform ni noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83954 1.7.1.1 14-3-3 protein isoform omega noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83950 1.7.1.1 14-3-3 protein isoform phi noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83951 1.7.1.1 14-3-3 protein isoform theta noncompetitive inhibition with a preferential binding to the substrate-bound state of the enzyme 83952 1.7.1.1 14-3-3B protein - 36357 1.7.1.1 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone a photosynthetic electron flux inhibitor of photosystem I, causes 61% inhibition at 0.008 mM 16755 1.7.1.1 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid - 49695 1.7.1.1 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide a NO scavenger 220841 1.7.1.1 3-(3,4-dichlorophenyl)-1,1-dimethylurea inhibits the post-translational light activation of nitrate reducate 29457 1.7.1.1 3-(3,4-dichlorophenyl)-1,1-dimethylurea a photosynthetic electron flux inhibitor of photosystem II, causes 51% inhibition at 0.001 mM 29457 1.7.1.1 adenine inhibition of the recombinant FAD domain 144 1.7.1.1 adenosine inhibition of the recombinant FAD domain 122 1.7.1.1 adenosine 5'-diphosphoribose dead-end inhibition 29704 1.7.1.1 adenosine 5'-diphosphoribose inhibition of the recombinant FAD domain 29704 1.7.1.1 ADP competitive with ADP 13 1.7.1.1 ADP inhibition of the recombinant FAD domain 13 1.7.1.1 Aminooxyacetate - 1374 1.7.1.1 AMP inhibition of the recombinant FAD domain 30 1.7.1.1 ATP at low pH, the presence of ATP alone in the incubation medium is sufficient to inactivate nitrate reductase 4 1.7.1.1 azide 1 mM sodium azide, 90% inhibition of nitrate reduction; sodium azide 230 1.7.1.1 azide sodium azide 230 1.7.1.1 azide inhibition of full and nitrate-reducing partial activities 230 1.7.1.1 Bromophenol blue noncompetitive versus NADH 5945 1.7.1.1 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 15 1.7.1.1 Carbamoyl phosphate competitive 440 1.7.1.1 Cd2+ 0.002 mM, 40% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration 52 1.7.1.1 Cl- alters the observed Mo(V) lineshape, mixed-type inhibitor, decreases both NADH:nitrate reductase and reduced methyl viologen:nitrate reductase activities 141 1.7.1.1 Co2+ 1 mM, strong inhibition 23 1.7.1.1 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 135355 1.7.1.1 Cr3+ 0.002 mM, 20% inhibition, 10 mM nitrilotriacetic acid does not protect 895 1.7.1.1 Cr6+ 0.001 mM, 62% inhibition, 10 mM nitrilotriacetic acid does not protect 4686 1.7.1.1 Cu after 24 h activity is reduced by 21.5%, 36% and 46% at 1 mM, 10 mM and 100 mM of Cu, respectively 460 1.7.1.1 Cu2+ potent inhibitor, inhibition can be abolished by prior chelation of the metal by EDTA 19 1.7.1.1 Cu2+ 1 mM, strong inhibition 19 1.7.1.1 Cu2+ 0.001 mM, 76% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration 19 1.7.1.1 Cyanate - 1376 1.7.1.1 cyanide - 118 1.7.1.1 cyanide mechanism of reactivation of cyanide-inactivated nitrate reductase by flavins in light 118 1.7.1.1 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 118 1.7.1.1 cyanide reactivation by incubation with oxidant systems after inactivation by treatment with NADH and cyanide 118 1.7.1.1 cyanide sodium azide 118 1.7.1.1 cyanide inhibition of full and nitrate-reducing partial activities 118 1.7.1.1 cyanide potent inhibitor 118 1.7.1.1 dicoumarol competitive towards NADH 754 1.7.1.1 dithiothreitol rate of inactivation is increased by NAD+, but not by NADP+ 45 1.7.1.1 Fe2+ potent inhibitor, inhibition can be abolished by prior chelation of the metal by EDTA 25 1.7.1.1 Fe3+ less potent inhibitor, effect cannot reversed by EDTA 70 1.7.1.1 ferricyanide inhibition of the recombinant FAD domain 132 1.7.1.1 ferrocytochrome c inactivation in a biphasic reaction, immune to inactivation during turnover with nitrate 530 1.7.1.1 glutamine 1 mM, decrease of activity 755 1.7.1.1 hydroxylamine - 85 1.7.1.1 hydroxylamine NO3-, cyanate, carbamoyl phosphate and azide protect from inactivation. Photoreactivation in presence of flavins, early inhibition appears to be competitive versus NO3- 85 1.7.1.1 hydroxylamine interacts with reduced cytochrome b557 during catalysis of the enzyme 85 1.7.1.1 KCN 0.1 mM, complete inhibition 161 1.7.1.1 menadione inhibits nitrate reductase 240 1.7.1.1 methyl methanethiosulfonate - 2346 1.7.1.1 methyl methanethiosulfonate inactivation is concentration independent 2346 1.7.1.1 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 6 1.7.1.1 Mg2+ no inhibition 6 1.7.1.1 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 6 1.7.1.1 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 6 1.7.1.1 MgCl2 0.1-5 mM, strong, both cytosolic and membrane-bound isozyme 196 1.7.1.1 MgCl2 10 mM, 75% decrease of activity 196 1.7.1.1 Mn2+ less potent inhibitor, effect cannot be reversed by EDTA 11 1.7.1.1 Mn2+ 1 mM, 27% inhibition 11 1.7.1.1 MoO42- 1 mM, strong inhibition 2413 1.7.1.1 additional information purification of a NADH-nitrate reductase inhibitor from young leaves of Glycine max, that causes a reversible inhibition 2 1.7.1.1 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 2 1.7.1.1 additional information inhibition by monospecific anti-nitrate reductase rabbit serum 2 1.7.1.1 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 2 1.7.1.1 additional information maize root inactivating enzyme inactivates pea leaf nitrate reductase 2 1.7.1.1 additional information maize root inactivating enzyme inactivates NADH:cytochrome c reductase at a greater rate than FADH2:nitrate reductase 2 1.7.1.1 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 2 1.7.1.1 additional information not inhibitory: ammonium, glutamine 2 1.7.1.1 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 2 1.7.1.1 additional information increasing level of salinity causes decrease in enzyme activity 2 1.7.1.1 additional information the enzyme is insensitive to oxygen 2 1.7.1.1 additional information the 14-3-3A protein and the 14-3-3C protein are functionally not capable to inhibit nitrate reductase 2 1.7.1.1 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 2 1.7.1.1 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 2 1.7.1.1 mutant G216S of 14-3-3A protein - 36358 1.7.1.1 N-ethylmaleimide 1 mM, complete inhibition 49 1.7.1.1 NaCl uncompetitive for nitrate and NADH 42 1.7.1.1 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% 42 1.7.1.1 NaCl 100 mM 42 1.7.1.1 NAD+ product inhibition 7 1.7.1.1 NAD+ - 7 1.7.1.1 NAD+ competitive towards NADH 7 1.7.1.1 NAD+ inactivation in presence of thiol compounds is enhanced by cyanide ions and can be reversed by ferricyanide 7 1.7.1.1 NAD+ inhibition of the recombinant FAD domain 7 1.7.1.1 NADH inactivation in a biphasic reaction, immune to inactivation during turnover with nitrate 8 1.7.1.1 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 8 1.7.1.1 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 8 1.7.1.1 NADH nitrate protects 8 1.7.1.1 NADH p-hydroxymercuribenzoate causes the appearance of an FAD-requirement for inactivation by NADH of FMNH2-nitrate reductase 8 1.7.1.1 NADPH nitrate protects 5 1.7.1.1 NaN3 0.1 mM, complete inhibition 238 1.7.1.1 NEM - 89 1.7.1.1 NEM inhibition of full and NADH-utilizing partial activities 89 1.7.1.1 NH4+ - 54 1.7.1.1 Ni2+ up to 0.1 mM, not inhibitory, 1 mM, 20% residual activity 38 1.7.1.1 nicotinamide inhibition of the recombinant FAD domain 267 1.7.1.1 nitrite product inhibition 168 1.7.1.1 nitrite competitive towards nitrate 168 1.7.1.1 nitrite - 168 1.7.1.1 NMN inhibition of the recombinant FAD domain 775 1.7.1.1 NO2- 10 mM, 65% inhibition 852 1.7.1.1 O-Methoxylamine - 94527 1.7.1.1 o-phenanthroline 1 mM, complete inhibition 239 1.7.1.1 p-chloromercuribenzoic acid 0.01 mM, complete inhibition 614 1.7.1.1 p-hydroxymercuribenzoate - 98 1.7.1.1 p-hydroxymercuribenzoate inactivation of NADH:nitrate reductase activity, no loss of bromphenol blue: nitrate reductase activity 98 1.7.1.1 p-hydroxymercuribenzoate dissapearance of NADH-diaphorase activity 98 1.7.1.1 p-hydroxymercuribenzoate inhibition of full and NADH-utilizing partial activities 98 1.7.1.1 Pb2+ less potent inhibitor, effect cannot reversed by EDTA 139 1.7.1.1 Pb2+ 0.002 mM, 60% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration 139 1.7.1.1 PCMB - 78 1.7.1.1 PCMB inactivation is concentration independent 78 1.7.1.1 phosphate 25 mM, increases activity with a nitrate concentration of 2 mM, decreases activity with a nitrate concentration of 0.1 mM 16 1.7.1.1 potassium ferricyanide preincubation with potassium ferricyanide inactivates nitrate reductase 2283 1.7.1.1 pyridoxal 5'-phosphate - 32 1.7.1.1 pyridoxal 5'-phosphate uncompetitive with nitrate 32 1.7.1.1 sodium nitroprusside a NO donor 1483 1.7.1.1 thiocyanate dead-end inhibition 931 1.7.1.1 thiocyanate - 931 1.7.1.1 VO3- 1 mM, strong inhibition 12727 1.7.1.1 Zn after 24 h activity is reduced by 11%, 19% and 21% at 1 mM, 10 mM and 100 mM of Cr, respectively 932 1.7.1.1 Zn2+ potent inhibitor, inhibition can be abolished by prior chelation of the metal by EDTA 14 1.7.1.1 Zn2+ 1 mM, strong inhibition 14 1.7.1.1 Zn2+ 0.004 mM, 60% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration 14