1.1.1.40 (NH4)2SO4 at high concentrations 399 1.1.1.40 (S)-malate substrate inhibition 200 1.1.1.40 (S)-malate an increase to malate concentration of 10 mM decreases the specific activity of rHVME1 by almost 50% 200 1.1.1.40 (S)-malate - 200 1.1.1.40 1-methylenecyclopropan-trans-2,3-dicarboxylic acid - 217318 1.1.1.40 1-methylenecyclopropane inhibits at 10 mM 217317 1.1.1.40 2'-AMP competitive 771 1.1.1.40 2,3-Butanedione pseudo-first-order loss of oxidative decarboxylase activity 1001 1.1.1.40 2-Ketoglutarate 34% inhibition at 2 mM 5098 1.1.1.40 2-mercaptoethanol inactivation in absence of Mg2+ 63 1.1.1.40 2-oxoglutarate strong 34 1.1.1.40 2-oxoglutarate competitive 34 1.1.1.40 2-oxoglutarate inhibition of isozyme NADP-ME2 34 1.1.1.40 2-oxoglutarate slight inhibition at 2 mM 34 1.1.1.40 3-(pyridin-2-yl)-6-[(5,6,7,8-tetrahydronaphthalen-2-yl)methyl][1,2,4]triazolo[3,4-b][1,3,4]thiadiazole ATR7-010 256610 1.1.1.40 5'-AMP competitive 236 1.1.1.40 acetyl phosphate slight inhibition at 2 mM 358 1.1.1.40 acetyl-CoA inhibition is much more pronounced in the mitochondrial enzyme than in the cytosolic enzyme and occurs at physiological acetyl-CoA concentrations 29 1.1.1.40 acetyl-CoA 40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2 29 1.1.1.40 acetyl-CoA inhibits isozyme NADP-ME1 29 1.1.1.40 acetyl-CoA - 29 1.1.1.40 acetyl-CoA acetyl-CoA (0.1 mM) exerts the greatest inhibitory effect leading to a residual activity of 24% 29 1.1.1.40 acetyl-CoA enzyme inhibition by acetyl-CoA is relieved by increasing CoASH concentrations 29 1.1.1.40 adenosine 2'-phosphate - 43703 1.1.1.40 ADP - 13 1.1.1.40 ADP 83% inhibition at 2 mM 13 1.1.1.40 ADP slight inhibition at 2 mM 13 1.1.1.40 AMP 41% inhibition at 5 mM 30 1.1.1.40 AMP 75% inhibition at 2 mM 30 1.1.1.40 arsenite weak 397 1.1.1.40 aspartate - 724 1.1.1.40 ATP non-competitive versus L-malate 4 1.1.1.40 ATP 27% inhibition at 0.2 mM 4 1.1.1.40 ATP 83% inhibition at 2 mM 4 1.1.1.40 ATP 20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2 4 1.1.1.40 ATP - 4 1.1.1.40 ATP weak inhibitor 4 1.1.1.40 ATP 10% inhibition of the wild-type enzyme at 3.0 mM in presence of NAD+, no inhibition in presence of NADP+, inhibition of mutant enzymes by ATP inpresence of NAD+ or NADP+ 4 1.1.1.40 ATP ATP at 2 mM inhibits the enzyme by 50%, but the activity is completely recovered if Mg2+ concentration increases to 5 mM 4 1.1.1.40 ATP slight inhibition at 2 mM 4 1.1.1.40 Ca2+ - 15 1.1.1.40 Ca2+ complete inhibition at 5 mM 15 1.1.1.40 Ca2+ great inhibition 15 1.1.1.40 cAMP 10% inhibition at 5 mM 268 1.1.1.40 cAMP slight inhibition at 1 mM 268 1.1.1.40 Cd2+ in the presence of Mn2+, Cd2+ ions almost completely inhibit the enzyme activity (5.9% residual activity) 52 1.1.1.40 citrate competitive, 61% inhibition at 5 mM 131 1.1.1.40 citrate competitive 131 1.1.1.40 Citric acid inhibits all PtNADP-ME activities significantly 1714 1.1.1.40 CO2 product inhibition, uncompetitive with respect to L-malate and NADP+, 39% inhibition at 25 mM 28 1.1.1.40 Co2+ - 23 1.1.1.40 Co2+ about 90% activity at 0.5 mM 23 1.1.1.40 Co2+ great inhibition 23 1.1.1.40 CoA 30% inhibition of isozyme NADP-ME1 at 2 mM 18 1.1.1.40 CoA activities of PtNADP-ME1, PtNADP-ME2 and PtNADPME4 proteins are inhibited 18 1.1.1.40 CoA slight inhibition at 1 mM 18 1.1.1.40 Cu2+ 3 mM, weak 19 1.1.1.40 Cu2+ complete inhibition at 0.1 mM, competitive to Mg2+ and Mn2+, enzyme inhibition leads to reduced lipid biosynthesis and accumulation of citric acid, quantitative overview 19 1.1.1.40 Cu2+ strong inhibition 19 1.1.1.40 Cu2+ complete inhibition at 5 mM 19 1.1.1.40 Cu2+-ascorbate rapid inactivation by generation of reactive oxygen species at pH 5.0, Fe2+ can substitute for Cu2+, Cu2+ or ascorbate alone are not effective, azide, 1,4-diazabicyclo-(2.2.2.)octane, histidine and imidazole protect against inhibition, the substrates L-malate and NADP+ and EDTA protect almost completely, loss of activity is accompanied with cleavage of the protein into 4 fragments of 14-55 kDa 122919 1.1.1.40 CuCl2 about 40% loss of activity within 60 min 347 1.1.1.40 D-fructose PtNADP-ME1 117 1.1.1.40 D-fructose-1,6-bisphosphate 13% inhibition at 5 mM 1895 1.1.1.40 D-fructose-1,6-bisphosphate when assayed at malate concentrations of 0.2 mM, D-fructose-1,6-bisphosphate inhibits the enzyme by a 49% over the control activity 1895 1.1.1.40 D-glucose 6-phosphate 40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2 105 1.1.1.40 D-Glucose-6-phosphate - 2838 1.1.1.40 D-malate - 1139 1.1.1.40 D-Tartrate - 7181 1.1.1.40 Diamide 2 mM, time-dependent decrease in activity reaching about 40% of initial activity after 60 min. In presence of dithiothreitol, a complete recovery is observed after 90 min. Enzyme oxidation decreases the catalytic activity. No severe loss of protein secondary structure takes place after oxidation; about 40% loss of activity within 60 min 2482 1.1.1.40 Diethylamine NONOate 35% inhibition at 5 mM 53154 1.1.1.40 diphenyliodonium chloride weak 93228 1.1.1.40 diphosphate diphosphate at 2 mM inhibits the enzyme by 50%, but the activity is completely recovered if Mg2+ concentration increases to 5 mM 17 1.1.1.40 EDTA - 21 1.1.1.40 embonic acid - 256608 1.1.1.40 Fe2+ - 25 1.1.1.40 Fe2+-ascorbate rapid inactivation 122920 1.1.1.40 fumarate at high concentration 170 1.1.1.40 fumarate 20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2 170 1.1.1.40 fumarate inhibits isozymes NADP-ME1 , NADP-ME3 and NADP-ME4 170 1.1.1.40 fumarate - 170 1.1.1.40 GDP 13% inhibition at 5 mM 53 1.1.1.40 glutamate - 297 1.1.1.40 glutamine slight inhibition at 5 mM 755 1.1.1.40 Glutarate inhibits at 10 mM 545 1.1.1.40 glutathione strongly inactivates in absence of Mg2+ 44 1.1.1.40 glyoxylate - 101 1.1.1.40 glyoxylate competitive inhibition, about 60% activity at 2 mM 101 1.1.1.40 glyoxylate competitive inhibition 101 1.1.1.40 H2O2 83% inhibition at 0.25 mM, 91.1% inhibition at 0.5 mM 22 1.1.1.40 Hg2+ 0.0005 mM, almost complete inhibition 33 1.1.1.40 Hydroxypyruvate hydroxypyruvate at 1 mM inhibits the enzyme activity by 45% 389 1.1.1.40 iodoacetate weak 93 1.1.1.40 Iodosobenzoate 1 mM, time-dependent decrease in activity reaching about 40% of initial activity after 60 min; about 40% loss of activity within 60 min 3856 1.1.1.40 L-aspartate competitive, 94% inhibition at 10 mM 97 1.1.1.40 L-malate pH 7.0, high concentration 247 1.1.1.40 L-Tartrate - 1874 1.1.1.40 Magnaporthe oryzae effector AVR-Pii - 212599 1.1.1.40 malate substrate inhibition 283 1.1.1.40 malate no inhibition at pH 7.0 283 1.1.1.40 malate inhibition at pH 7.0 283 1.1.1.40 malate excess of malate inhibits the oxidative decarboxylation catalyzed by the cytosolic enzyme at pH 7.0, and below, decarboxylation catalyzed by mitochondrial enzyme is unaffected by the substrate 283 1.1.1.40 malate inhibition at high concentrations at pH 7.0, but not at pH 8.0 283 1.1.1.40 malate inhibition of isozyme NADP-ME1 at pH 7.0 283 1.1.1.40 malate the enzyme is inhibited by high malate concentration at pH 7.0 283 1.1.1.40 Maleate the cis isomer of fumarate, inhibition of isozyme NADP-ME2 575 1.1.1.40 malonate - 392 1.1.1.40 malonate inhibition of isozyme NADP-ME2 392 1.1.1.40 malonyl-CoA inhibition of mitochondrial enzyme and cytosolic enzyme to a much lower extent than with acetyl-CoA 76 1.1.1.40 Mg2+ mitochondrial enzyme, decarboxylation reaction, above 6 mM 6 1.1.1.40 Mg2+ activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding, Km is 0.19 mM 6 1.1.1.40 Mg2+ about 80% activity at 0.5 mM 6 1.1.1.40 additional information feedback inhibition is reduced by illumination 2 1.1.1.40 additional information glutamine is a poor inhibitor 2 1.1.1.40 additional information no substrate inhibition of isozyme Hvme3 at 10 mM L-malate 2 1.1.1.40 additional information no inhibition of isozyme NADP-ME2 by aspartate and malate 2 1.1.1.40 additional information the expression levels of isozyme NADP-ME1 in leaves clearly decreases to the lowest point at 6 h following application of abscisic acid (0.2 mM), when treated with 4°C, NaCl, and PEG, NADP-ME1 is down-regulated and low temperature treatment is more distinct; with respect to isozyme NADP-ME2, the expression levels are reduced by abscisic acid and salicylic acid treatments, in the salicylic acid treatment, the expression amounts of NADP-ME2 decrease to least at 3 h treatment, then begin to ascend till 6 h and again start to descend till 24 h treatment 2 1.1.1.40 additional information cytosolic NADP-ME expression in roots decreases with development, decreased levels of expression of cytosolic NADP-ME is observed in roots after incubating in solutions of Na2CO3 at pH 11.0 or NaHCO3 at pH 6.5; cytosolic NADP-ME is not inhibited by high malate concentrations at pH 7.0; NADP-ME is not affected by acetyl-CoA, CoA, pyruvate, L-alanine, alpha-ketoglutarate, glycerol-3-phosphate, 3-phospho-glycerate, and citrate 2 1.1.1.40 additional information keeping plants in CO2-free air suppresses the activities of NADP-ME 2 1.1.1.40 additional information ZmnonC4-NADP-ME activity is not significantly modified by any chemical oxidant in 60 min 2 1.1.1.40 additional information no inhibition of isozyme NADP-ME2 by tartrate 2 1.1.1.40 additional information not inhibited by ATP, ADP, AMP, propionyl-COA, acetyl-CoA, CoA, succinate, L-glutamate, L-aspartate, isocitrate, citrate, pyruvate, D-fructose 6-phosphate, D-glucose 6-phosphate, and 2-oxoglutarate 2 1.1.1.40 additional information ATR4-003 (3-(4-methoxyphenyl)-2-methyl-5-([(4-methylpyrimidin-2-yl)sulfanyl]methyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one) and ATR6-001 ([1-amino-5-(morpholin-4-yl)-6,7,8,9-tetrahydrothieno[2,3-c]isoquinolin-2-yl](piperidin-1-yl)methanone) do not inhibitenzyme activity up to a concentration of 0.02 mM 2 1.1.1.40 additional information peroxynitrite does not affect the enzyme even at a high concentration of 5 mM 3-morpholinosydnonimine 2 1.1.1.40 Na2S the enzyme activity is inhibited by up to 29-32% using 2 and 5 mM Na2S as H2S donor 2087 1.1.1.40 NaCl at high concentrations 42 1.1.1.40 NaCl in the presence of 50 mM KCl, 50 mM NaCl inhibits the enzyme activity by 40% 42 1.1.1.40 NAD+ weak 7 1.1.1.40 NADP+ substrate inhibition 10 1.1.1.40 NADPH product inhibition, competitive with respect to L-malate and NADP+ 5 1.1.1.40 Ni2+ about 50% activity at 0.5 mM 38 1.1.1.40 NPD389 - 256607 1.1.1.40 o-Iodosobenzoate strong 2092 1.1.1.40 oxalate - 185 1.1.1.40 oxalate 51% inhibition at 1 mM 185 1.1.1.40 oxalate inhibition is decreased by light exposure 185 1.1.1.40 oxaloacetate strong 57 1.1.1.40 oxaloacetate - 57 1.1.1.40 oxaloacetate competitive, 70% inhibition at 2 mM 57 1.1.1.40 oxaloacetate competitive 57 1.1.1.40 oxaloacetate competitive inhibition, about 25% activity at 2 mM 57 1.1.1.40 oxaloacetate feedback inhibition 57 1.1.1.40 oxaloacetic acid 60% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2 2862 1.1.1.40 oxaloacetic acid inhibits all PtNADP-ME activities significantly 2862 1.1.1.40 p-mercuribenzoate strong 686 1.1.1.40 peroxynitrite peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration at Tyr-73 to 3-nitrotyrosine 1220 1.1.1.40 Phenylglyoxal pseudo-first-order loss of oxidative decarboxylase activity 301 1.1.1.40 phosphate 35% inhibition at 5 mM 16 1.1.1.40 phosphoenolpyruvate 39% inhibition at 5 mM 51 1.1.1.40 phosphoenolpyruvate competitive, 82% inhibition at 2 mM 51 1.1.1.40 phosphoenolpyruvate slight inhibition at 1 mM 51 1.1.1.40 pyruvate competitive 31 1.1.1.40 pyruvate non-competitive inhibition 31 1.1.1.40 pyruvate product inhibition, competitive with respect to L-malate, 16% inhibition at 5 mM 31 1.1.1.40 pyruvate inhibition is decreased by light exposure 31 1.1.1.40 pyruvate 22% inhibition at 2 mM 31 1.1.1.40 pyruvate 20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2 31 1.1.1.40 pyruvate - 31 1.1.1.40 S-nitrosocysteine 35% inhibition at 5 mM 8516 1.1.1.40 sesamol added to the medium, inhibits best at 9 mM; a specific inhibitor of the enzyme; strong inhibition at 10 mM 171910 1.1.1.40 sesamol - 171910 1.1.1.40 Sn2+ 1 mM Sn2+ ions reduce the enzyme activity by 31% 413 1.1.1.40 SO32- in decarboxylation of malate: partially competitive with respect to malate, in carboxylation of pyruvate: fully competitive for CO2 or HCO3- 902 1.1.1.40 succinate slight inhibition at high concentrations 58 1.1.1.40 succinate competitive, 28% inhibition at 5 mM 58 1.1.1.40 succinate inhibition of isozyme NADP-ME2 58 1.1.1.40 succinate - 58 1.1.1.40 sulfite - 92 1.1.1.40 Tartrate inhibits at 10 mM 762 1.1.1.40 Tartronate - 4283 1.1.1.40 Tartronate noncompetitive inhibitor with respect to L-malate 4283 1.1.1.40 Trypsin digests the mutant enzymes, while the wild-type enzyme is protected in the presence of Mn2+, because a specific cutting site in the Lys352-Gly-Arg354 region is able to generate a unique polypeptide with Mr of 37 kDa, and this polypeptide is resistant to further digestion 393 1.1.1.40 Urea inactivation at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, overview 116 1.1.1.40 Zn2+ - 14 1.1.1.40 Zn2+ strong inhibition 14 1.1.1.40 Zn2+ about 10% activity at 5 mM 14 1.1.1.40 Zn2+ great inhibition 14