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(NH4)2SO4
-
at high concentrations
1-methylenecyclopropan-trans-2,3-dicarboxylic acid
-
1-methylenecyclopropane
inhibits at 10 mM
2,3-Butanedione
Pigeon
-
pseudo-first-order loss of oxidative decarboxylase activity
2-Ketoglutarate
-
34% inhibition at 2 mM
2-mercaptoethanol
-
inactivation in absence of Mg2+
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
acetyl phosphate
-
slight inhibition at 2 mM
adenosine 2'-phosphate
Pigeon
-
-
Cd2+
-
in the presence of Mn2+, Cd2+ ions almost completely inhibit the enzyme activity (5.9% residual activity)
Citric acid
-
inhibits all PtNADP-ME activities significantly
CO2
-
product inhibition, uncompetitive with respect to L-malate and NADP+, 39% inhibition at 25 mM
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
CuCl2
about 40% loss of activity within 60 min
D-fructose-1,6-bisphosphate
D-glucose 6-phosphate
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
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
Diethylamine NONOate
-
35% inhibition at 5 mM
diphenyliodonium chloride
Pigeon
-
weak
diphosphate
-
diphosphate at 2 mM inhibits the enzyme by 50%, but the activity is completely recovered if Mg2+ concentration increases to 5 mM
Fe2+-ascorbate
-
rapid inactivation
GDP
-
13% inhibition at 5 mM
glutamine
-
slight inhibition at 5 mM
Glutarate
inhibits at 10 mM
glutathione
-
strongly inactivates in absence of Mg2+
H2O2
-
83% inhibition at 0.25 mM, 91.1% inhibition at 0.5 mM
Hg2+
Pigeon
-
0.0005 mM, almost complete inhibition
Hydroxypyruvate
-
hydroxypyruvate at 1 mM inhibits the enzyme activity by 45%
iodoacetate
Pigeon
-
weak
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
L-aspartate
-
competitive, 94% inhibition at 10 mM
L-malate
pH 7.0, high concentration
Magnaporthe oryzae effector AVR-Pii
-
-
-
Maleate
-
the cis isomer of fumarate, inhibition of isozyme NADP-ME2
malonyl-CoA
-
inhibition of mitochondrial enzyme and cytosolic enzyme to a much lower extent than with acetyl-CoA
Na2S
-
the enzyme activity is inhibited by up to 29-32% using 2 and 5 mM Na2S as H2S donor
NADP+
-
substrate inhibition
NADPH
-
product inhibition, competitive with respect to L-malate and NADP+
Ni2+
-
about 50% activity at 0.5 mM
o-Iodosobenzoate
Pigeon
-
strong
p-mercuribenzoate
Pigeon
-
strong
peroxynitrite
-
peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration at Tyr-73 to 3-nitrotyrosine
Phenylglyoxal
Pigeon
-
pseudo-first-order loss of oxidative decarboxylase activity
phosphate
-
35% inhibition at 5 mM
S-nitrosocysteine
-
35% inhibition at 5 mM
Sn2+
-
1 mM Sn2+ ions reduce the enzyme activity by 31%
SO32-
-
in decarboxylation of malate: partially competitive with respect to malate, in carboxylation of pyruvate: fully competitive for CO2 or HCO3-
Tartrate
inhibits at 10 mM
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
-
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
(S)-malate
-
substrate inhibition
(S)-malate
an increase to malate concentration of 10 mM decreases the specific activity of rHVME1 by almost 50%
2-oxoglutarate
-
inhibition of isozyme NADP-ME2
2-oxoglutarate
-
slight inhibition at 2 mM
2-oxoglutarate
-
competitive
acetyl-CoA
-
inhibits isozyme NADP-ME1
acetyl-CoA
-
enzyme inhibition by acetyl-CoA is relieved by increasing CoASH concentrations
acetyl-CoA
-
acetyl-CoA (0.1 mM) exerts the greatest inhibitory effect leading to a residual activity of 24%
acetyl-CoA
40% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
acetyl-CoA
-
inhibition is much more pronounced in the mitochondrial enzyme than in the cytosolic enzyme and occurs at physiological acetyl-CoA concentrations
ADP
-
slight inhibition at 2 mM
ADP
-
83% inhibition at 2 mM
AMP
-
75% inhibition at 2 mM
AMP
-
41% inhibition at 5 mM
ATP
-
ATP
-
slight inhibition at 2 mM
ATP
-
non-competitive versus L-malate
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+
ATP
-
83% inhibition at 2 mM
ATP
-
ATP at 2 mM inhibits the enzyme by 50%, but the activity is completely recovered if Mg2+ concentration increases to 5 mM
ATP
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
ATP
27% inhibition at 0.2 mM
Ca2+
-
Ca2+
-
complete inhibition at 5 mM
cAMP
-
slight inhibition at 1 mM
cAMP
-
10% inhibition at 5 mM
citrate
-
competitive, 61% inhibition at 5 mM
Co2+
-
Co2+
-
about 90% activity at 0.5 mM
CoA
-
slight inhibition at 1 mM
CoA
30% inhibition of isozyme NADP-ME1 at 2 mM
CoA
-
activities of PtNADP-ME1, PtNADP-ME2 and PtNADPME4 proteins are inhibited
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
Cu2+
-
complete inhibition at 5 mM
D-fructose-1,6-bisphosphate
-
13% inhibition at 5 mM
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
fumarate
-
inhibits isozymes NADP-ME1 , NADP-ME3 and NADP-ME4
fumarate
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
fumarate
-
at high concentration
glyoxylate
-
competitive inhibition, about 60% activity at 2 mM
glyoxylate
competitive inhibition
malate
-
no inhibition at pH 7.0
malate
-
no inhibition at pH 7.0
malate
-
inhibition at pH 7.0
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
malate
-
no inhibition at pH 7.0
malate
inhibition of isozyme NADP-ME1 at pH 7.0
malate
-
the enzyme is inhibited by high malate concentration at pH 7.0
malate
Pigeon
-
substrate inhibition
malate
-
the enzyme is inhibited by high malate concentration at pH 7.0
malate
-
no inhibition at pH 7.0
malate
-
inhibition at pH 7.0
malate
-
inhibition at high concentrations at pH 7.0, but not at pH 8.0
malate
-
the enzyme is inhibited by high malate concentration at pH 7.0
malonate
-
inhibition of isozyme NADP-ME2
Mg2+
-
activates at up to 4 mM, inhibition above, probably due to blockage of substrate binding, Km is 0.19 mM
Mg2+
-
about 80% activity at 0.5 mM
Mg2+
-
mitochondrial enzyme, decarboxylation reaction, above 6 mM
NaCl
-
at high concentrations
NaCl
-
in the presence of 50 mM KCl, 50 mM NaCl inhibits the enzyme activity by 40%
oxalate
-
-
oxalate
-
51% inhibition at 1 mM
oxalate
-
inhibition is decreased by light exposure
oxaloacetate
-
oxaloacetate
-
competitive, 70% inhibition at 2 mM
oxaloacetate
-
competitive inhibition, about 25% activity at 2 mM
oxaloacetate
feedback inhibition
oxaloacetate
-
competitive
oxaloacetate
-
competitive
oxaloacetic acid
60% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
oxaloacetic acid
-
inhibits all PtNADP-ME activities significantly
phosphoenolpyruvate
-
slight inhibition at 1 mM
phosphoenolpyruvate
-
competitive, 82% inhibition at 2 mM
phosphoenolpyruvate
-
39% inhibition at 5 mM
pyruvate
-
-
pyruvate
-
22% inhibition at 2 mM
pyruvate
20% inhibition of isozyme NADP-ME1 at 2 mM; inhibition of isozyme NADP-ME2
pyruvate
-
product inhibition, competitive with respect to L-malate, 16% inhibition at 5 mM
pyruvate
-
non-competitive inhibition
pyruvate
-
inhibition is decreased by light exposure
sesamol
added to the medium, inhibits best at 9 mM; a specific inhibitor of the enzyme; strong inhibition at 10 mM
succinate
-
succinate
-
competitive, 28% inhibition at 5 mM
succinate
inhibition of isozyme NADP-ME2
succinate
-
slight inhibition at high concentrations
Tartronate
-
noncompetitive inhibitor with respect to L-malate
Zn2+
-
-
Zn2+
-
about 10% activity at 5 mM
additional information
-
no inhibition of isozyme NADP-ME2 by tartrate
-
additional information
-
peroxynitrite does not affect the enzyme even at a high concentration of 5 mM 3-morpholinosydnonimine
-
additional information
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
additional information
-
no substrate inhibition of isozyme Hvme3 at 10 mM L-malate
-
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
-
additional information
-
glutamine is a poor inhibitor
-
additional information
Mnium undulatum
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
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
-
additional information
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
-
no inhibition of isozyme NADP-ME2 by aspartate and malate
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
additional information
-
keeping plants in CO2-free air suppresses the activities of NADP-ME
-
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
-
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
-
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
-
additional information
-
feedback inhibition is reduced by illumination
-
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
-
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
-
additional information
-
ZmnonC4-NADP-ME activity is not significantly modified by any chemical oxidant in 60 min
-
additional information
ZmnonC4-NADP-ME activity is not significantly modified by any chemical oxidant in 60 min
-