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2-fluoro-2-phosphonoacetohydroxamate
competitive inhibitor
3-aminoenolpyruvate phosphate
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3-hydroxy-2-nitro-1-phosphonopropane
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3-hydroxypropionic acid phosphate
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CaCl2
5 mM, about 10% residual activity
Cr2+
leads to complete inhibition at 10 mM
Cu2+
leads to complete inhibition at 10 mM
cumene hydroperoxide
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1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h
D-2,3-dihydroxyisobutyric acid 2-phosphate
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D-erythro-2,3-dihydroxybutyric acid 2-phosphate
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D-erythro-2,3-dihydroxybutyric acid 3-phosphate
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D-glycerate-2-phosphate
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mixed-type inhibition in the binding of D-glycerate-2-phosphate and D-phosphoglycerate mutase to the D-glycerate-2-phosphate binding site on the enolase in absence of D-glycerate-2,3-diphosphate, inhibition is almost fully reverted by D-glycerate-2,3-diphosphate
D-glyceric acid 3-phosphate
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D-lactic acid phosphate
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D-tartronate semialdehyde phosphate
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diphosphate
inhibits natural enolase and recombinant protein
Hg2+
leads to complete inhibition at 10 mM
hydrogen peroxide
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inhibitory at 0.25%, at pH 7
iodoacetamide
binds to cysteine residues
MgCl2
inhibitory above 50 mM
Na+
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50% inhibition around 0.3-0.4 M
p19ras
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when full-length p19ras and C-terminal region are bound to NSE, it inhibits the enzymatic activity of NSE, p19ras interacts with enolase alpha and represses its enzymatic activity in vitro
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peracetic acid
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1% residual activity after treatment with 4 mM peracetic acid at 25°C and pH 7 for 15 min
phosphonoacetohydroxamate
PO43-
mimics the phosphate group of substrate
SO42-
induces a complete closure of catalytic site loops
tert-butyl hydroperoxide
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1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50°C and pH 7 for 3 h
2-phosphoglycerate
presence of 0.8 mM 2-phosphoglycerate abolished the binding of beta,beta-enolase to tubulin, kinetics shown
2-phosphoglycerate
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competitive
2-phosphoglycerate
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competitive
2-phosphoglycerate
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substrate inhibition
4-hydroxy-2-nonenal
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acrolein
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citrate
competitive
citrate
KX452941
1 mM, 11.5% inhibition
EDTA
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F-
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noncompetitive in the presence of phosphate, competitive in the absence of phosphate
F-
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in presence of phosphate, competitive
F-
non-competitive inhibition without phosphate and in presence of 1 mM phosphate, competitive inhibition in presence of 20 mM phosphate
F-
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noncompetitive inhibition below 10 mM, competitive above 10 mM
F-
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quasi-irreverible inhibition above 0.01 mM
F-
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in absence of phosphate noncompetitive inhibition up to 10 mM F-, competitive inhibition in presence of 0.5 mM phosphate
fluoride
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the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
fluoride
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the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
KCl
monomeric form
KCl
activating at 50-200 mM, inhibitory above
Li+
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Li+
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noncompetitive with either 2-phosphoglycerate or Mg2+
Li+
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liver enzyme is severely inhibited, muscle enzyme is moderately inhibited
methylglyoxal
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incubation of0.015 mM enzyme with 2 mM, 3.1 mM and 4.34 mM methylglyoxal in 100 mM phosphate buffer pH 7.4 for 3 h causes the loss a 32%, 55% and 82% of initial specific activity, respectively. Inhibition of enolase by methylglyoxal and formation of enolase-derived glycation products arises more effectively in slight alkaline conditions and in the presence of inorganic phosphate
Mg2+
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at high concentrations
Mg2+
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inhibitory in excess
Mg2+
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Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
Mg2+
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inhibitory in excess
Mg2+
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inhibitory at higher concentrations
Mg2+
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inhibitor above 1 mM, N207A, H159A, H159N and H159F mutants are stimulated at this concentration
Mg2+
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Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
Mg2+
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inhibitory at higher concentrations
Mn2+
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inhibitory in excess
Mn2+
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inhibitory in excess
NaCl
inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form
NaCl
inhibitory above 50 mM
NaClO4
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inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation
NaClO4
E414L mutant is more sensitive to inactivation than the wild-type enzyme
NaClO4
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enolase at 19.4 mM after incubation in 0.2 M NaClO4, has 32% of its original activity and is 21% octameric. Following a 24 h dialysis against buffer, the protein is 77% octameric and has 74% of its original activity
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
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at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
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at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
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competitive inhibitor of enolase
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphonoacetohydroxamate
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phosphonoacetohydroxamate
preference for formation of hybrid Zn2+/Mn2+ complexes with enolase, in vitro activity of the complexed enolase in presence of phosphonoacetohydroxamate investigated by crystallography and electron paramagnetic resonance spectroscopy
phosphonoacetohydroxamate
retains open tunnel from catalytic site to protein surface, offers possibilities for drug development
trans-2-nonenal
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Zn2+
-
inhibitory in excess
Zn2+
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inhibitory in excess
additional information
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the muscle-specific enolase is used as a model enzyme for inhibition analysis by acrolein, 4-hydroxy-2-nonenal, and trans-2-nonenal, incubation for 1-24 h at 25°C, 37°C, and 45°C, overview. The compounds show inhibition effectivity in the following descending order: inhibition degree of enolase activity occurred in following order: 4-hydroxy-2-nonenal, acrolein, methylglyoxal, trans-2-nonenal, overview
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additional information
antibodies against enolase inhibits up to 60% of plasminogen binding
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additional information
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antibodies against enolase inhibits up to 60% of plasminogen binding
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additional information
recombinant enolase inhibits activity of purified dextransucrase
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additional information
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recombinant enolase inhibits activity of purified dextransucrase
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additional information
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no inhibition by NEM and iodoacetate
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additional information
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no inhibition by SH-reagents
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additional information
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additional information
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inhibition of enolase by fluoride in combination with phosphate can influence glycolysis and so reduce acid production of even growth rate, thereby leading to potential anticariogenic effects
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additional information
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the muscle-specific enolase is used as a model enzyme for inhibition analysis by acrolein, 4-hydroxy-2-nonenal, and trans-2-nonenal, incubation for 1-24 h at 25°C, 37°C, and 45°C, overview. The compounds show inhibition effectivity in the following descending order: inhibition degree of enolase activity occurred in following order: 4-hydroxy-2-nonenal, acrolein, methylglyoxal, trans-2-nonenal, overview
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