4.2.1.11 2-fluoro-2-phosphonoacetohydroxamate competitive inhibitor 66802 4.2.1.11 2-phosphoglycerate substrate inhibition 750 4.2.1.11 2-phosphoglycerate competitive 750 4.2.1.11 2-phosphoglycerate presence of 0.8 mM 2-phosphoglycerate abolished the binding of beta,beta-enolase to tubulin, kinetics shown 750 4.2.1.11 3-aminoenolpyruvate phosphate - 197354 4.2.1.11 3-hydroxy-2-nitro-1-phosphonopropane - 118338 4.2.1.11 3-hydroxypropionic acid phosphate - 91478 4.2.1.11 4-hydroxy-2-nonenal - 1426 4.2.1.11 acrolein - 1198 4.2.1.11 Ca2+ - 15 4.2.1.11 CaCl2 5 mM, about 10% residual activity 218 4.2.1.11 citrate competitive 131 4.2.1.11 citrate 1 mM, 11.5% inhibition 131 4.2.1.11 Cr2+ leads to complete inhibition at 10 mM 1919 4.2.1.11 Cu2+ leads to complete inhibition at 10 mM 19 4.2.1.11 cumene hydroperoxide 1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h 814 4.2.1.11 D-2,3-dihydroxyisobutyric acid 2-phosphate - 97853 4.2.1.11 D-erythro-2,3-dihydroxybutyric acid 2-phosphate - 96335 4.2.1.11 D-erythro-2,3-dihydroxybutyric acid 3-phosphate - 96336 4.2.1.11 D-glycerate-2-phosphate 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 93049 4.2.1.11 D-glyceric acid 3-phosphate - 93050 4.2.1.11 D-lactic acid phosphate - 96355 4.2.1.11 D-tartronate semialdehyde phosphate - 156852 4.2.1.11 diphosphate inhibits natural enolase and recombinant protein 17 4.2.1.11 EDTA - 21 4.2.1.11 EDTA 1 mM 21 4.2.1.11 F- - 174 4.2.1.11 F- in presence of phosphate, competitive 174 4.2.1.11 F- noncompetitive inhibition below 10 mM, competitive above 10 mM 174 4.2.1.11 F- quasi-irreverible inhibition above 0.01 mM 174 4.2.1.11 F- in absence of phosphate noncompetitive inhibition up to 10 mM F-, competitive inhibition in presence of 0.5 mM phosphate 174 4.2.1.11 F- noncompetitive in the presence of phosphate, competitive in the absence of phosphate 174 4.2.1.11 F- non-competitive inhibition without phosphate and in presence of 1 mM phosphate, competitive inhibition in presence of 20 mM phosphate 174 4.2.1.11 fluoride the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level 407 4.2.1.11 Hg2+ leads to complete inhibition at 10 mM 33 4.2.1.11 hydrogen peroxide inhibitory at 0.25%, at pH 7 1126 4.2.1.11 iodoacetamide binds to cysteine residues 67 4.2.1.11 KBr monomeric form 2746 4.2.1.11 KCl monomeric form 79 4.2.1.11 KCl activating at 50-200 mM, inhibitory above 79 4.2.1.11 Li+ noncompetitive with either 2-phosphoglycerate or Mg2+ 152 4.2.1.11 Li+ liver enzyme is severely inhibited, muscle enzyme is moderately inhibited 152 4.2.1.11 Li+ - 152 4.2.1.11 methylglyoxal 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 322 4.2.1.11 methylglyoxal - 322 4.2.1.11 Mg2+ inhibitor above 1 mM, N207A, H159A, H159N and H159F mutants are stimulated at this concentration 6 4.2.1.11 Mg2+ inhibitory at higher concentrations 6 4.2.1.11 Mg2+ at high concentrations 6 4.2.1.11 Mg2+ above 2 mM 6 4.2.1.11 Mg2+ inhibitory in excess 6 4.2.1.11 Mg2+ Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate 6 4.2.1.11 MgCl2 inhibitory above 50 mM 196 4.2.1.11 Mn2+ inhibitory in excess 11 4.2.1.11 monofluorophosphate - 96787 4.2.1.11 additional information no inhibition by SH-reagents 2 4.2.1.11 additional information - 2 4.2.1.11 additional information no inhibition by NEM and iodoacetate 2 4.2.1.11 additional information 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 2 4.2.1.11 additional information recombinant enolase inhibits activity of purified dextransucrase 2 4.2.1.11 additional information antibodies against enolase inhibits up to 60% of plasminogen binding 2 4.2.1.11 additional information 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 2 4.2.1.11 Na+ 50% inhibition around 0.3-0.4 M 59 4.2.1.11 Na2PO3F - 98132 4.2.1.11 NaCl inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form 42 4.2.1.11 NaCl inhibitory above 50 mM 42 4.2.1.11 NaClO4 inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation 9230 4.2.1.11 NaClO4 E414L mutant is more sensitive to inactivation than the wild-type enzyme 9230 4.2.1.11 NaClO4 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 9230 4.2.1.11 p19ras 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 155910 4.2.1.11 peracetic acid 1% residual activity after treatment with 4 mM peracetic acid at 25°C and pH 7 for 15 min 4679 4.2.1.11 phosphate - 16 4.2.1.11 phosphate competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate 16 4.2.1.11 phosphate at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition 16 4.2.1.11 phosphate competitive inhibitor of enolase 16 4.2.1.11 phosphonoacetohydroxamate - 16215 4.2.1.11 phosphonoacetohydroxamate retains open tunnel from catalytic site to protein surface, offers possibilities for drug development 16215 4.2.1.11 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 16215 4.2.1.11 PO43- mimics the phosphate group of substrate 867 4.2.1.11 SO42- induces a complete closure of catalytic site loops 245 4.2.1.11 tert-butyl hydroperoxide 1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50°C and pH 7 for 3 h 624 4.2.1.11 trans-2-nonenal - 2372 4.2.1.11 Zn2+ inhibitory in excess 14