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0.107
-
pH 7.5, 37°C, activity in undialyzed cell extracts
0.41
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crude extract, at pH 7.8
0.79
-
substrate: 2-phospho-D-glycerate, 50°C, pH not specified in the publication, enzyme from starch-grown cells
0.9
-
crude extract, at pH 6.8
1.1
-
H159N mutant, pH 7.8, 21ºC
1.9
-
H159F mutant, pH 7.8, 21ºC
10050
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Zn2+
11.29
substrate phosphoenolpyruvate, 22°C, pH not specified in the publication
111
room temperature, pH 7.5, MgCl2, KCl, 2-phosphoglyceric acid
1118
-
dimeric enzyme form
15.87
purified recombinant enzyme, substrate phosphoenolpyruvate, pH 7.4, 20°C
197.4
-
plastidic isoenzyme
23.2
-
SPM2, 0.25% Triton X-100
248
-
N207A mutant, pH 7.8, 21ºC
252.4
-
cytosolic isoenzyme
260
-
pH 8.1, room temperature
3.3
-
H159A mutant, pH 7.8, 21ºC
30
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2-phospho-D-glycerate, pH 7.4, 20°C, Tris/HCl
30.71
substrate 2-phospho-D-glycerate, 22°C, pH not specified in the publication
31.2
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after 76.1fold purification, at pH 7.8
35.81
purified recombinant enzyme, substrate 2-phospho-D-glycerate, pH 7.4, 20°C
3909
purifed recombinant enzyme, pH 8.5, 37°C, no metal ion added
442
-
wild type, pH 7.8, 21ºC
60.72
pH not specified in the publication, temperature not specified in the publication
67
recombinant wild-type enzyme, pH 7.1, 25ºC
67.4
-
enolase from synaptosomal cytoplasm
700
-
pH 7.6, temperature not specified in the publication
75
-
after 83fold purification, at pH 6.8
77
recombinant E414L mutant, pH 7.1, 25ºC
9091
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Mg2+
918
-
monomeric enzyme form
51
-
-
60 - 70
-
pH 7.4
87
-
muscle enolase
additional information
functional activity of recombinant protein shown, immunogenicity determined by ELISA and Western Blot using different sera, natural infection of humans by Anisakis simplex larvae lacks sufficient antigenic stimuli
additional information
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functional activity of recombinant protein shown, immunogenicity determined by ELISA and Western Blot using different sera, natural infection of humans by Anisakis simplex larvae lacks sufficient antigenic stimuli
additional information
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Vmax at 37°C and pH 6.8: 0.506 micromol/min/mg for the recombinant protein
additional information
spectrophotometric assay described, generation of reaction products determined by NMR
additional information
biological activity shown, enzyme activity comparable to those of Candida
additional information
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biological activity shown, enzyme activity comparable to those of Candida
additional information
binding studies of recombinant protein to human plasminogen confirms properties as host-interacting molecule
additional information
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binding studies of recombinant protein to human plasminogen confirms properties as host-interacting molecule
additional information
multifunctional role of enolase, participation in the parasitic invasion process and in the control of gene regulation
additional information
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multifunctional role of enolase, participation in the parasitic invasion process and in the control of gene regulation
additional information
-
-
additional information
-
-
additional information
additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
additional information
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additional and independent function beyond glycolytic enzyme function, association of enolase to the RNA degrasome, role in RNA metabolism predicted
additional information
spectrophotometric assay described, D-ribulose 1-phosphate and 5-methylthio-D-ribulose 1-phosphate in the presence of limiting 5-methylthio-D-ribulose 1-phosphate dehydratase analyzed, enzyme concentrations from 0.1 to 10 microM used
additional information
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-
additional information
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-
additional information
enolase activity measured spectrophotometrically by following the change in phosphoenolpyruvate concentration, substrate concentrations up to 0.3 mM for 2-phospho-D-glycerate and up to 2 mM for phosphoenolpyruvate
additional information
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enolase activity measured spectrophotometrically by following the change in phosphoenolpyruvate concentration, substrate concentrations up to 0.3 mM for 2-phospho-D-glycerate and up to 2 mM for phosphoenolpyruvate
additional information
recombinant enolase has plasminogen binding activity, similarities to nine amino-acid internal plasminogen-binding motif of Streptococcus pneumoniae, enolase as one of the plasminogen receptors in the parasite predicted
additional information
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recombinant enolase has plasminogen binding activity, similarities to nine amino-acid internal plasminogen-binding motif of Streptococcus pneumoniae, enolase as one of the plasminogen receptors in the parasite predicted
additional information
activity of recombinant protein spectrophotometrically measured by conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, substrate concentrations of 3 mM
additional information
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activity of recombinant protein spectrophotometrically measured by conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, substrate concentrations of 3 mM
additional information
-
-
additional information
enzyme activity measured with the natural substrate 2-phospho-D-glycerate, conversion of reaction products determined by spectroscopy, kinetics of binding studies to tubulin by ELISA and surface plasmon resonance
additional information
enzyme activity measured with the natural substrate 2-phospho-D-glycerate, conversion of reaction products determined by spectroscopy, kinetics of binding studies to tubulin by ELISA and surface plasmon resonance
additional information
enzyme activity tested, kinetics of binding studies to tubulin estimated by ELISA and surface plasmon resonance, association of beta,beta enolase to microtubules in differentiating myotubes but not in myoblasts
additional information
enzyme activity tested, kinetics of binding studies to tubulin estimated by ELISA and surface plasmon resonance, association of beta,beta enolase to microtubules in differentiating myotubes but not in myoblasts
additional information
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31.2 nmol 2-PGA converted/min/36nM enolase
additional information
kinetic properties of monomeric and dimeric forms of recombinant enolase compared, enzyme activity measured spectrophotometrically by monitoring formation of 2-phospho-D-glycerate, dimeric structure not essential for catalysis, monomeric form indicates a 3fold lower activity
additional information
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kinetic properties of monomeric and dimeric forms of recombinant enolase compared, enzyme activity measured spectrophotometrically by monitoring formation of 2-phospho-D-glycerate, dimeric structure not essential for catalysis, monomeric form indicates a 3fold lower activity
additional information
recombinant enolase protein of Plasmodium falciparum can protect mice against malaria, assay described
additional information
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recombinant enolase protein of Plasmodium falciparum can protect mice against malaria, assay described
additional information
Plasmodium yoeliie XL17
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the recombinant enolase of Plasmodium falciparum can protect mice infected with the lethal strain 17XL against malaria, assay described
additional information
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-
additional information
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additional and independent function beyond glycolytic enzyme function, involvement in mitochondrial tRNA targeting, depletion of enolase inhibits tRNA import in vivo, activity of enolase as an alternative molecular chaperone suggested
additional information
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
additional information
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binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
additional information
enzyme activity monitored by following the conversion of phosphoenolpyruvate to 2-phospho-D-glycerate, specific activities of the variants, relative to wildtype enolase, are 0.1% for G157D and 0.01% for G376E
additional information
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enzyme activity monitored by following the conversion of phosphoenolpyruvate to 2-phospho-D-glycerate, specific activities of the variants, relative to wildtype enolase, are 0.1% for G157D and 0.01% for G376E
additional information
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
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in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
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enolase shows the same specific activity (110 U/mg) in Tris-acetate or Tris-HCl buffers, whereas the specific activity is diminished (70 U/mg) in phosphate buffer
additional information
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-
additional information
purified recombinant enolase has plasminogen binding activity, analyzed by flow cytometry
additional information
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purified recombinant enolase has plasminogen binding activity, analyzed by flow cytometry
additional information
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his-tagged recombinant protein has the same activity than the wild type
additional information
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additional information
activity assay of recombinant protein
additional information
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activity assay of recombinant protein