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(25R)-3beta-hydroxycholest-5-en-27-oate
?
(Z)-3-chloro-2-phosphoenolpyruvate + OH-
?
-
wild-type enzyme catalyzes hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
2,3-diketohexane 1-phosphate
?
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
3-phospho-D-erythronate
?
-
-
-
-
?
3-phospho-D-glycerate
?
-
-
-
-
?
D-tartronate semialdehyde phosphate
?
D-tartronate semialdehyde-2-phosphate
?
-
substrate analogue that changes its spectrum while bound to the enzyme
-
?
phosphoenolpyruvate
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
additional information
?
-
(25R)-3beta-hydroxycholest-5-en-27-oate
?
-
-
-
-
?
(25R)-3beta-hydroxycholest-5-en-27-oate
?
-
-
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
-
-
?
2,3-diketohexane 1-phosphate
?
alternate substrate, C1 proton abstraction
-
-
?
2,3-diketohexane 1-phosphate
?
alternate substrate, C1 proton abstraction
-
-
?
2,3-diketohexane 1-phosphate
?
alternate substrate, C1 proton abstraction
-
-
?
2-phospho-D-glycerate
?
-
the enzyme is a plasminogen binding protein
-
-
?
2-phospho-D-glycerate
?
-
beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
-
-
?
2-phospho-D-glycerate
?
-
enzyme of glycolysis
-
-
?
2-phospho-D-glycerate
?
-
age-related changes in the properties of the enzyme
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
studies on host-trematode relationships, properties of enolase as a host-interacting molecule analyzed
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
substrate binding in pre-catalytic state and during catalysis, recombinant enzyme, overview
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
665313, 665841, 666023, 666046, 701578, 701579, 702856, 703010, 703739, 704073, 704848, 705257, 705386, 706638, 706933 -
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
interaction studies between alpha,alpha enolase and tubulin, co-localization studies with microtubules
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
additional functions apart from glycolytic function of enolase tested
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
kinetic and structural properties of monomeric and dimeric forms of recombinant enolase of Plasmodium falciparum compared
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17
-
additional functions apart from glycolytic function of enolase tested, vaccination studies in mice
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17 17XL
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17 17XL
-
additional functions apart from glycolytic function of enolase tested, vaccination studies in mice
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
the enzyme probably functions in sugar fermentation pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
in vitro studies on catalytic, divalent cation binding sites
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
influence on exchange of amino acid residues on structure, dissociation and function of enolase analyzed
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
separated role of enolase besides function in glycolysis, stimulation of vacuole fusion and involvement in protein trafficking to vacuoles determined
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
plasminogen-binding activity besides metabolic function
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces mutans
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces pneumoniae
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
KX452941
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
structural analysis
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
D-tartronate semialdehyde phosphate
?
-
slowly-reacting strongly bound chromophoric substrate
-
-
?
D-tartronate semialdehyde phosphate
?
-
slowly-reacting strongly bound chromophoric substrate
-
-
?
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
?
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
-
-
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
-
-
r
additional information
?
-
enzymes is confirmed by total proteome analysis of glycerol-grown cells
-
-
?
additional information
?
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
-
His-tagged recombinant enolase protein shows a high affinity for human plasminogen
-
-
?
additional information
?
-
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
?
additional information
?
-
-
enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions
-
-
?
additional information
?
-
-
enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions
-
-
?
additional information
?
-
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
?
additional information
?
-
-
enolase shows plasminogen-binding activity
-
-
?
additional information
?
-
-
enolase acts as a DNA methyltransferase 2 inhibitor. Enolase interacts with Ehmeth, and modulates its activity under conditions of glucose starvation inhibiting the binding of Ehmeth and human DNA methyltransferase 2 to Entamoeba histolytica MRS2 DNA
-
-
?
additional information
?
-
-
ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256
-
-
?
additional information
?
-
-
the enzyme binds plasminogen
-
-
?
additional information
?
-
-
the enzyme binds plasminogen
-
-
?
additional information
?
-
the enzyme binds to plasminogen
-
-
?
additional information
?
-
-
the enzyme binds to plasminogen
-
-
?
additional information
?
-
the enzyme binds to plasminogen
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin
-
-
r
additional information
?
-
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway
-
-
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
methionine salvage pathway
-
-
?
2-phospho-D-glycerate
?
-
the enzyme is a plasminogen binding protein
-
-
?
2-phospho-D-glycerate
?
-
beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
-
-
?
2-phospho-D-glycerate
?
-
enzyme of glycolysis
-
-
?
2-phospho-D-glycerate
?
-
age-related changes in the properties of the enzyme
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17 17XL
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
the enzyme probably functions in sugar fermentation pathway
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces mutans
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces pneumoniae
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
additional information
?
-
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
?
additional information
?
-
-
plasminogen bound to recombinant enolase can be converted to active plasmin
-
-
?
additional information
?
-
-
enolase shows plasminogen-binding activity
-
-
?
additional information
?
-
-
enolase acts as a DNA methyltransferase 2 inhibitor. Enolase interacts with Ehmeth, and modulates its activity under conditions of glucose starvation inhibiting the binding of Ehmeth and human DNA methyltransferase 2 to Entamoeba histolytica MRS2 DNA
-
-
?
additional information
?
-
-
ENOA has C-terminal lysines predominantly responsible for plasminogen activation, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Al3+
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 68.8% of the maximal activity with 10 mM Mg2+
Cd2+
-
14% of the activation with Mg2+
Cu2+
-
20% of the activiation with Mg2+
KBr
dimeric form 10-20% activated, monomeric form strongly inhibited
Ni2+
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.5% of the maximal activity with 10 mM Mg2+
Co2+
-
absolute requirement for divalent metal ions, 9% of the activity with Mg2+
Co2+
-
less than 40% of the activation with Mg2+
Co2+
-
activates in 0.1 M KCl, maximum activity at 0.0035 mM. Maximum of 4 Co2+ ions are bound per dimer
K+
-
activates, best at 2 mM
K+
-
slightly activating effect
KCl
dimeric form 10-20% activated, monomeric form strongly inhibited
KCl
-
required for maximal activity
KCl
activating at 50-200 mM, inhibitory above
Mg2+
the highest activation rate of the enzymatic activity is reached at 5 mM Mg2+ and remains unchanged up to 25 mM
Mg2+
activates, optimally at 10 mM
Mg2+
-
required for activity, can be replaced by Mn2+ or Zn2+, but lower activity is observed
Mg2+
Km value 2.5 mM at 25°C, 1.9 mM at 80°C, respectively
Mg2+
-
activates, best at 10 mM
Mg2+
-
optimal concentration: 1 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
two magnesium ions per subunit are required for catalytic activity
Mg2+
coordinated in catalytic site of enolase
Mg2+
-
Mg2+ is the strongest enolase activating metal. Binding of two Mg2+ ions is essential
Mg2+
-
required for activity
Mg2+
activation by 2 Mg2+ molecules per subunit, one conformational and one catalytic ion
Mg2+
-
maximal specific activity with respect to 2-phospho-D-glycerate is achieved in the presence of 1 mM Mg2+, in the presence of 0.1 mM MnSO4 or 0.24 mM ZnSO4 (i.e. the optimal concentrations of Mn2+ or Zn2+ ions), only 46% and 14%, respectively, of the activity determined for the Mg2+-stimulated reaction is found
Mg2+
-
required for activity, the optimum concentration is 3 mM
Mg2+
-
maximal specific activity with respect to 2-phospho-D-glycerate is achieved in the presence of 1 mM Mg2+, in the presence of 0.1 mM MnSO4 or 0.24 mM ZnSO4 (i.e. the optimal concentrations of Mn2+ or Zn2+ ions), only 46% and 14%, respectively, of the activity determined for the Mg2+-stimulated reaction is found
Mg2+
each monomer is binding a single Mg2+ cofactor
Mg2+
activity depends on, optimal concentration for activity between 1 mM and 2 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
-
three binding sites, binding at the first two is required for activity, binding at the third site is inhibitory
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
protects enolases of yeast and of rabbit muscle but not of Plasmodium falciparum from dissociation in presence of imidazol
Mg2+
metal ion required, equally active in presence of Mg2+ and Mn2+, 1 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
-
required for activity
Mg2+
two ions are necessary for activity, shows inhibition at high concentration
Mg2+
-
enolase is activated by low concentrations of Mg2+
Mg2+
-
physiological cofactor
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
-
activation by several divalent cation, Mg2+ is most effective
Mg2+
-
at pH 6.8, Km for liver enzyme: 0.67 mM, Km for muscle enzyme: 1.33 mM at pH 7.4, Km for liver enolase: 0.42 mM, Km for muscle enolase: 0.25 mM
Mg2+
-
absolute requirement for divalent metal ions, Mg2+ is most effective
Mg2+
essential for activity, high concentrations are inhibitory
Mn2+
-
required
Mn2+
can partially substitute for Mg2+ or Zn2+ at 10 mM showing 90.4% of the maximal activity with 10 mM Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
absolute requirement for divalent metal ions
Mn2+
-
46% of the activation with Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
metal ion required, equally active in presence of Mg2+ and Mn2+, 1 mM
Mn2+
-
Km for the cytoplasmic isoenzyme: 1.2 mM
Mn2+
-
absolute requirement for divalent metal ions
Mn2+
-
Km for the plastidic isoenzyme: 1.4 mM
Mn2+
-
10% of the activation with Mg2+
Mn2+
can replace Mg2+, mechanistic study using electron paramagnetic resonance
Mn2+
catalytic binding sites analyzed in vitro
Mn2+
-
can also bind and activate the enzyme
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
19% of the activation with Mg2+
Zn2+
activates, optimally at 10 mM, best activating metal ion
Zn2+
-
optimal concentration: 1 mM
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
absolute requirement for divalent metal ions, 35% of the activation with Mg2+
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
can replace Mg2+, mechanistic study using electron paramagnetic resonance
Zn2+
catalytic binding sites analyzed in vitro
Zn2+
-
can also bind and activate the enzyme
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
12% of the activation with Mg2+
additional information
57% of maximal activity without metal ion compared to Mg2+ at 10 mM
additional information
-
57% of maximal activity without metal ion compared to Mg2+ at 10 mM
additional information
-
enolase 1 is a metalloenzyme with an absolute requirement for divalent metal ions
additional information
-
Ca2+, Ba2+, Sr2+, Hg2+, Pb2+, and Be2+ are not capable of activating the enzyme
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2-fluoro-2-phosphonoacetohydroxamate
competitive inhibitor
3-aminoenolpyruvate phosphate
-
-
3-hydroxy-2-nitro-1-phosphonopropane
-
3-hydroxypropionic acid phosphate
-
-
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
-
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
-
-
D-erythro-2,3-dihydroxybutyric acid 2-phosphate
-
-
D-erythro-2,3-dihydroxybutyric acid 3-phosphate
-
-
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
D-glyceric acid 3-phosphate
-
-
D-lactic acid phosphate
-
-
D-tartronate semialdehyde phosphate
-
-
diphosphate
inhibits natural enolase and recombinant protein
Hg2+
leads to complete inhibition at 10 mM
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
iodoacetamide
binds to cysteine residues
MgCl2
inhibitory above 50 mM
Na+
-
50% inhibition around 0.3-0.4 M
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
-
peracetic acid
-
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
-
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
-
competitive
2-phosphoglycerate
-
competitive
2-phosphoglycerate
-
substrate inhibition
4-hydroxy-2-nonenal
-
-
acrolein
-
-
citrate
competitive
citrate
KX452941
1 mM, 11.5% inhibition
EDTA
-
-
F-
-
noncompetitive in the presence of phosphate, competitive in the absence of phosphate
F-
-
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-
-
noncompetitive inhibition below 10 mM, competitive above 10 mM
F-
-
quasi-irreverible inhibition above 0.01 mM
F-
-
in absence of phosphate noncompetitive inhibition up to 10 mM F-, competitive inhibition in presence of 0.5 mM phosphate
fluoride
-
the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
fluoride
-
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+
-
-
Li+
-
noncompetitive with either 2-phosphoglycerate or Mg2+
Li+
-
liver enzyme is severely inhibited, muscle enzyme is moderately inhibited
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
Mg2+
-
at high concentrations
Mg2+
-
inhibitory in excess
Mg2+
-
Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
Mg2+
-
inhibitory in excess
Mg2+
-
inhibitory at higher concentrations
Mg2+
-
inhibitor above 1 mM, N207A, H159A, H159N and H159F mutants are stimulated at this concentration
Mg2+
-
Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
Mg2+
-
inhibitory at higher concentrations
Mn2+
-
inhibitory in excess
Mn2+
-
inhibitory in excess
NaCl
inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form
NaCl
inhibitory above 50 mM
NaClO4
-
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
-
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
-
competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
-
at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
-
at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
-
competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
-
competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
-
competitive inhibitor of enolase
phosphate
-
competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphonoacetohydroxamate
-
-
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
-
-
Zn2+
-
inhibitory in excess
Zn2+
-
inhibitory in excess
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
-
additional information
antibodies against enolase inhibits up to 60% of plasminogen binding
-
additional information
-
antibodies against enolase inhibits up to 60% of plasminogen binding
-
additional information
recombinant enolase inhibits activity of purified dextransucrase
-
additional information
-
recombinant enolase inhibits activity of purified dextransucrase
-
additional information
-
no inhibition by NEM and iodoacetate
-
additional information
-
no inhibition by SH-reagents
-
additional information
-
-
-
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
-
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
-
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0.041 - 0.25
(25R)-3beta-hydroxycholest-5-en-27-oate
0.025 - 6.053
2-phospho-D-glycerate
0.39 - 1.281
3-phospho-D-glycerate
0.07 - 43
phosphoenolpyruvate
additional information
2-phospho-D-glycerate
0.041
(25R)-3beta-hydroxycholest-5-en-27-oate
-
2-phospho-D-glycerate
0.25
(25R)-3beta-hydroxycholest-5-en-27-oate
-
phosphoenolpyruvate
0.025
2-phospho-D-glycerate
-
plastidic isoenzyme
0.029
2-phospho-D-glycerate
-
brain enolase I, brain enolase II, brain enolase III
0.03
2-phospho-D-glycerate
pH 6.5, 80°C
0.031
2-phospho-D-glycerate
-
at 0.035 mM Co2+
0.032
2-phospho-D-glycerate
-
in presence of 1 mM Mg2+, native enzyme
0.03205
2-phospho-D-glycerate
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.036
2-phospho-D-glycerate
-
enolase III
0.038
2-phospho-D-glycerate
-
-
0.038
2-phospho-D-glycerate
-
muscle enolase
0.04
2-phospho-D-glycerate
-
recombinant, dimeric enzyme
0.04
2-phospho-D-glycerate
-
recombinant, His-tagged, hexameric enzyme
0.043
2-phospho-D-glycerate
wild type, 25°C, Mg2+, pH 7.5
0.04482
2-phospho-D-glycerate
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.045
2-phospho-D-glycerate
-
-
0.045
2-phospho-D-glycerate
-
enolase II
0.05
2-phospho-D-glycerate
-
-
0.05
2-phospho-D-glycerate
-
-
0.05
2-phospho-D-glycerate
recombinant protein
0.05
2-phospho-D-glycerate
K345A/N80D/N126D, 25°C, Mg2+, pH 7.5
0.054
2-phospho-D-glycerate
pH 7.6, 25ºC
0.057
2-phospho-D-glycerate
-
enolase I
0.057
2-phospho-D-glycerate
N80D/N126D, 25°C, Mg2+, pH 7.5
0.05856
2-phospho-D-glycerate
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.06
2-phospho-D-glycerate
65°C, pH not specified in the publication
0.061
2-phospho-D-glycerate
-
-
0.061
2-phospho-D-glycerate
-
cytosolic isoenzyme
0.069
2-phospho-D-glycerate
-
-
0.07
2-phospho-D-glycerate
-
at 75°C
0.078
2-phospho-D-glycerate
-
-
0.08
2-phospho-D-glycerate
natural enolase
0.082
2-phospho-D-glycerate
-
at pH 8.0
0.086
2-phospho-D-glycerate
in 81 mM triethanolamine/HCl, pH 7.4, at 25°C
0.09
2-phospho-D-glycerate
-
pH 6.8, muscle enolase
0.09
2-phospho-D-glycerate
-
pH 7.4, liver enolase and muscle enolase
0.09
2-phospho-D-glycerate
KX452941
pH 7.0, 25°C
0.106
2-phospho-D-glycerate
1.5 mM MgCl2 in 50 mM Tris/HCl (pH 7.4), at 25°C
0.11
2-phospho-D-glycerate
-
mutant E168Q
0.12
2-phospho-D-glycerate
-
muscle enzyme
0.12
2-phospho-D-glycerate
-
mutant enzyme E211Q
0.131
2-phospho-D-glycerate
-
in presence of 1 mM Mg2+, mutant enzyme S39A
0.14
2-phospho-D-glycerate
-
liver enzyme
0.149
2-phospho-D-glycerate
-
at pH 7.0
0.16
2-phospho-D-glycerate
pH 6.5, 25°C
0.17
2-phospho-D-glycerate
-
pH 6.8, liver enolase
0.18
2-phospho-D-glycerate
80°C, pH not specified in the publication
0.199
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.2
2-phospho-D-glycerate
-
native enzyme, in the absence of methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.21
2-phospho-D-glycerate
37°C, in reaction buffer
0.22
2-phospho-D-glycerate
-
Y-NSE.H6
0.24
2-phospho-D-glycerate
-
R-NSE
0.25
2-phospho-D-glycerate
-
Y-NSE
0.3
2-phospho-D-glycerate
-
-
0.3
2-phospho-D-glycerate
-
wild type enzyme
0.38
2-phospho-D-glycerate
-
pH 6.8, 30ºC
0.4
2-phospho-D-glycerate
pH 8, 70°C
0.425
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
0.44
2-phospho-D-glycerate
-
in presence of 1 mM Mg2+
0.66
2-phospho-D-glycerate
-
glycated enzyme, in the presence of 40% (v/v) methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.68
2-phospho-D-glycerate
-
mutant K345A
0.71
2-phospho-D-glycerate
-
-
0.77
2-phospho-D-glycerate
22°C, pH not specified in the publication
1.1
2-phospho-D-glycerate
pH not specified in the publication, temperature not specified in the publication
1.5 - 2
2-phospho-D-glycerate
pH 7.0, temperature not specified in the publication
1.9
2-phospho-D-glycerate
in 100 mM HEPES buffer, pH 8.5, 7.7 mM KCl, 10 mM MgSO4, at 25°C
2
2-phospho-D-glycerate
pH 8.5, 25°C, recombinant enzyme
2
2-phospho-D-glycerate
-
50°C, pH not specified in the publication
2.47
2-phospho-D-glycerate
in 100 mM HEPES, 10 mM MgCl2, and 7.7 mM KCl, pH 7.0, at 37°C
2.61
2-phospho-D-glycerate
at pH 6.8
4.35
2-phospho-D-glycerate
-
-
6.053
2-phospho-D-glycerate
pH 7.0, 30°C
0.39
3-phospho-D-glycerate
-
at pH 7.0
1.281
3-phospho-D-glycerate
-
at pH 8.0
0.07
phosphoenolpyruvate
acitivity for monomers
0.11
phosphoenolpyruvate
-
-
0.11
phosphoenolpyruvate
-
-
0.14
phosphoenolpyruvate
-
enolase III
0.15
phosphoenolpyruvate
-
enolase I
0.17
phosphoenolpyruvate
-
pH 7.4, muscle enolase
0.18
phosphoenolpyruvate
-
at pH 8.0
0.19
phosphoenolpyruvate
-
enolase II
0.19
phosphoenolpyruvate
-
pH 6.8, liver enolase
0.2
phosphoenolpyruvate
-
-
0.2
phosphoenolpyruvate
-
-
0.2
phosphoenolpyruvate
recombinant protein
0.21
phosphoenolpyruvate
natural enolase
0.244
phosphoenolpyruvate
pH 7.6, 25ºC
0.25
phosphoenolpyruvate
-
-
0.25
phosphoenolpyruvate
-
-
0.25
phosphoenolpyruvate
-
pH 7.4, liver enolase
0.28
phosphoenolpyruvate
activity for dimeric form
0.31
phosphoenolpyruvate
-
liver enzyme
0.33
phosphoenolpyruvate
-
pH 6.8, muscle enolase
0.37
phosphoenolpyruvate
-
muscle enzyme
0.392
phosphoenolpyruvate
80°C, pH not specified in the publication
0.534
phosphoenolpyruvate
-
at pH 7.0
0.538
phosphoenolpyruvate
65°C, pH not specified in the publication
0.58
phosphoenolpyruvate
-
native enzyme, in the absence of methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.6
phosphoenolpyruvate
22°C, pH not specified in the publication
0.657
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
0.702
phosphoenolpyruvate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.83
phosphoenolpyruvate
-
glycated enzyme, in the presence of 40% (v/v) methyglyoxal, in 50 mM imidazole-HCl buffer, pH 6.8, with 0.4 M KCl and 3 mM MgSO4
0.95
phosphoenolpyruvate
-
pH 6.8, 30ºC
2.6
phosphoenolpyruvate
-
plastidic isoenzyme
3.3
phosphoenolpyruvate
-
recombinant protein
7.2
phosphoenolpyruvate
-
cytosolic isoenzyme
43
phosphoenolpyruvate
E414L mutant enzyme, pH 7.1, 25ºC
additional information
2-phospho-D-glycerate
-
Km ranges between 0.047 mM and 0.130 mM between pH 6.0 and pH 8.6
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
temperature-dependence of Km-values
-
additional information
additional information
disruption of subunit-subunit interactions declines enzyme activity 3fold
-
additional information
additional information
-
disruption of subunit-subunit interactions declines enzyme activity 3fold
-
additional information
additional information
kinetic analysis, forward and reverse reaction, overview
-
additional information
additional information
-
kinetic analysis, forward and reverse reaction, overview
-
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0.0014
2-fluoro-2-phosphonoacetohydroxamate
at pH 7.2, binds in the same way as phosphoenolpyruvate and phosphonoacetohydroxamate
0.015
phosphonoacetohydroxamate
-
0.127
diphosphate
recombinant protein, substrate 2-phospho-D-glycerate
0.232
diphosphate
natural enolase, substrate 2-phospho-D-glycerate
0.238
diphosphate
natural enolase, substrate phosphoenolpyruvate
0.26
diphosphate
recombinant protein, substrate 2-phospho-D-glycerate
4.6
F-
in presence of 1 mM phosphate
5.4
F-
in absence of phosphate
9.2
F-
in presence of 20 mM phosphate
10
F-
-
pH 6.8, 30ºC, in the absence of phosphate
2.2
fluoride
-
at low phosphate concentrations (4-6 mM), in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
18.8
fluoride
-
at low phosphate concentrations (4-6 mM), in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.327
Mg2+
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.695
Mg2+
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
2.1
Mg2+
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
3.249
Mg2+
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
14.37
Mg2+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
1.266
Mn2+
-
in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
3.04
Mn2+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.32
phosphate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.9
phosphate
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in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
1.58
Zn2+
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
2.34
Zn2+
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in 50 mM imidazole-HCl buffer, pH 7.8, with 1 mM MgSO4, 0.4 M KCl
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0.107
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pH 7.5, 37°C, activity in undialyzed cell extracts
0.41
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crude extract, at pH 7.8
0.79
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substrate: 2-phospho-D-glycerate, 50°C, pH not specified in the publication, enzyme from starch-grown cells
0.9
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crude extract, at pH 6.8
1.1
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H159N mutant, pH 7.8, 21ºC
1.9
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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
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dimeric enzyme form
15.87
purified recombinant enzyme, substrate phosphoenolpyruvate, pH 7.4, 20°C
197.4
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plastidic isoenzyme
23.2
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SPM2, 0.25% Triton X-100
248
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N207A mutant, pH 7.8, 21ºC
252.4
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cytosolic isoenzyme
260
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pH 8.1, room temperature
3.3
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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
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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
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enolase from synaptosomal cytoplasm
700
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pH 7.6, temperature not specified in the publication
75
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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
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monomeric enzyme form
51
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60 - 70
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pH 7.4
87
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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
-
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
-
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
-
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
-
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
-
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
-
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
-
-
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
-
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
-
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
-
the recombinant enolase of Plasmodium falciparum can protect mice infected with the lethal strain 17XL against malaria, assay described
additional information
-
-
additional information
-
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
-
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
-
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
-
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
-
-
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
-
-
additional information
activity assay of recombinant protein
additional information
-
activity assay of recombinant protein
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enolase I
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expression is 2.38fold higher in the adult worms than in the cysticerci
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ENOA is upregulated
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ENOA is upregulated
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ENOA is upregulated
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expression is 2.38fold higher in the adult worms than in the cysticerci
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developing
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ENOA is upregulated
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ENOA is upregulated
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ENOA is upregulated
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of infected hosts Mesocricetus auratus and Rattus norvegicus, excretory and secretory products after infection analyzed
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ENOA is upregulated
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constitutive expression of gene LOS2
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ENOA is upregulated
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ENOA is upregulated
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ENOA is upregulated
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bladder wall of the metacestode
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ENOA is upregulated
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ENOA complexes with annexin A2, cytokeratin 8 and tissue-type plasminogen activator in raft membrane fractions of pancreatic cancer cells
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ENOA is upregulated
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constitutive expression of gene LOS2
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ENOA is upregulated
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ENOA is upregulated
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testicular, epididymal and ejaculated
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germinated
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constitutive expression of gene LOS2
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present in the teratocytes and released in the host haemocoel
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ENOA is upregulated
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enolase I
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human serum samples collected from residents living in areas of Eastern India, where Plasmodium falciparum is endemic, 96% reactivity of the recombinant enolase r-Pfren determined
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Plasmodium yoeliie XL17
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mice hosts, for SDS-PAGE and immunoblot analysis
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Plasmodium yoeliie XL17 17XL
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mice hosts, for SDS-PAGE and immunoblot analysis
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enolase 1 is only expressed in bradyzoites
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expression in the latent bradyzoite cyst stage
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the brain alpha,gamma and gamma,gamma forms are not detectable in the early embryonic stage and increase gradually during the development of the brain, whereas the alpha,alpha form exists at an almost constant level during development
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enolase I (alpha,alpha-enolase), enolase II (alpha,gamma-enolase), enolase III (gamma,gamma-enolase)
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enolase I (alpha,alpha-enolase), enolase II (alpha,gamma-enolase), enolase III (gamma,gamma-enolase)
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cell surface ENOA is enhanced
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4 d old
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strain B-512FMCM
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strain B-512FMCM
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back and hind legs
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enolase I and III
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adult worm
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enolase I
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L3 state
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enolase I
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hindlimb muscle
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contains only enolase III
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for in vivo binding studies to human plasminogen
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for in vivo binding studies to human plasminogen
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isolated after infection of 2-week-old White Leghorn PA12 chickens for 68 h, protein but not cDNA detected in the sporozoite stage, expression enhanced during the first schizogony
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isolated after infection of 2-week-old White Leghorn PA12 chickens for 68 h, protein but not cDNA detected in the sporozoite stage, expression enhanced during the first schizogony
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contains a single enzyme form
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beta,beta-enolase, complete switching from alpha,alpha enolase to beta,beta enolase during the period around hatching
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muscle-specific enolase
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alpha,beta heterodimer and beta,beta homodimer in striated muscle, interaction with tubulin during differentiation of muscle satellite cells but not in undifferentiated myoblasts, immobilized beta,beta-enolase interacts with tubulin in vitro
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satellite cell differentiation, alpha,alpha-enolase highly expressed during early ontogenesis, concentration of alpha,alpha-enolase in skeletal muscle varies from 0.1 mM to 0.01 mM until differentiation, binding affinity to tubulin is about 0.2 microM, alpha,beta heteroassociation with tubulin in muscle under physiological conditions
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muscle-specific enolase
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enolase I
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enolase 2 is only expressed in tachyzoites
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expression in the rapidly replicative tachyzoite stage
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recovered from liver, the enzyme expression in reduced in trophozoites continuously cultured in axenical conditions, semi-qiantitative RT-PCR expression analysis
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recovered from liver, the enzyme expression in reduced in trophozoites continuously cultured in axenical conditions, semi-qiantitative RT-PCR expression analysis
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additional information
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ENO1 is expressed in most heterotrophic tissues but not in the mesophyll of leaves
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additional information
PtrLOS2 expression in roots and stems is much higher than that in leaves under normal conditions, however, the expression of PtrLOS2 is upregulated in leaves, but downregulated in roots after cold treatments. The PtrLOS2 expression in stems is firstly up-regulated and then down-regulated after cold treatments
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additional information
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enolase expression analysis in adult worm, metacercaria, cercaria and egg. Csenolase is transcribed at the four life stages of Clonorchis sinensis while showing a significant higher expression level at the stage of adult worm
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additional information
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from mature cysts obtained from human stools
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additional information
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from mature cysts obtained from human stools
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additional information
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present in all human organs but at levels less than 3% of those found in human brain, with especially low levels in liver, kidney, and skeletal muscle, and with the highest level in adrenal and large intestine
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additional information
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tissue-specific expression of isozymes: ENOA is present in almost all adult tissues, beta-enolase is expressed in muscle tissues, and gamma-enolase is found in neurons and neuroendocrine tissues
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additional information
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the embryonic alpha,alpha isoform remains distributed in many adult cell types, wheras a transition towards beta,beta-isoform and gamma,gamma-isoform occurs in striated muscle cells and neurons respectively
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additional information
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enolase 1 is a glycolytic enzyme expressed in most tissues
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additional information
the enolase gene is highly expressed at 18-28 days of the life cycle, RT-PCR expression analysis
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additional information
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the enolase gene is highly expressed at 18-28 days of the life cycle, RT-PCR expression analysis
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additional information
enzyme is distributed in the periphery of calcareous corpuscles
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additional information
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enzyme is distributed in the periphery of calcareous corpuscles
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additional information
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5 isoenzymes, one isoenzyme form is present in all tissues tested, two additional forms are expressed in oocytes, embryos, adult liver and adult brain, two further forms are restricted to larval and adult muscle
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isozyme enolase 1
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caudal flagellum
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association of enolase with the food vacuole
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up to 7% of enolase activity associated with mitochondria, targeting towards the mitochondrial outer membrane, affinity to the mitochondrial surface more than 10fold higher for Eno2p than for Eno1p
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synaptic plasma membrane
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secreted enzyme associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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putative ENOA translocation mechanism, overview
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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secreted enzyme associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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Streptomyces mutans
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associated to the external surface of the parasite
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Streptomyces pneumoniae
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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associated to the external surface of the parasite
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partly localized inside the nucleus of sporozoites and schizonts, partly secreted, apex of the first generation of merozoites, relocalization inside sporozoites observed
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partly localized inside the nucleus of sporozoites and schizonts, partly secreted, apex of the first generation of merozoites, relocalization inside sporozoites observed
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surface-localization on merozoites determined by indirect immunofluorescence assay
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Plasmodium yoeliie XL17
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surface-localization on merozoites determined by indirect immunofluorescence assay
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Plasmodium yoeliie XL17 17XL
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surface-localization on merozoites determined by indirect immunofluorescence assay
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low amounts of surface-exposed enolase, determined on viable pneumococci, monoclonal and polyconal antibodies used
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isozyme enolase 2
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as part of the degradosome complex
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enzyme activity only in cytosolic fraction, inactive form detected in the microsomal fraction, membrane-association and localization at the external face of the plasma membrane determined by digitonin treatment and immunofluorescence studies
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microsomal fraction analyzed
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enzyme activity only in cytosolic fraction, inactive form detected in the microsomal fraction, membrane-association and localization at the external face of the plasma membrane determined by digitonin treatment and immunofluorescence studies
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microsomal fraction analyzed
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cytosolic fractions of myoblasts and myotubes, microtubule-association of alpha,alpha-enolase in undifferentiated myoblasts and in myotubes, also nuclear localization in myoblasts but not in myotubes determined, role of enolases in cytoskeletal dynamics during myoblast differentiation assumed
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nuclear localization in myoblasts not detected, direct interaction with microtubules and tubulin during myoblast differentiation identified, role in cytoskeletal dynamics during myoblast differentiation assumed
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small portion of enolase bound to vacuoles, in vitro stimulation of vacuole fusion determined
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secreted enzyme associated to the external surface of the parasite
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme
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secreted enzyme associated to the external surface of the parasite
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secreted enzyme
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secreted enzyme
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secreted enzyme
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brenda
Streptomyces mutans
-
secreted enzyme
-
brenda
Streptomyces pneumoniae
-
secreted enzyme
-
brenda
-
secreted enzyme
-
brenda
-
secreted enzyme
-
brenda
-
-
brenda
-
-
-
-
brenda
-
-
brenda
-
-
-
-
brenda
-
-
brenda
-
-
brenda
-
in some human cancer cell lines
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
-
brenda
-
-
brenda
-
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
brenda
-
enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
outer membrane vesicle
brenda
-
outer membrane vesicle
-
brenda
additional information
-
the enzyme is not exposed on the cell surface
-
brenda
additional information
-
the enzyme is not exposed on the cell surface
-
-
brenda
additional information
-
enolase as both an excretory/secretory product and a tegumental component of Clonorchis sinensis, immunohistochemical analysis
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
enolase is specifically located inside vesicles containing densely packed fibrilar material
-
brenda
additional information
-
enolase is specifically located inside vesicles containing densely packed fibrilar material
-
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
alpha-enolase is not detected in the nucleus
-
brenda
additional information
-
in breast, lung and pancreatic neoplasia, ENOA is localized on the surface of cancer cells, whereas in melanoma and nonsmall cell lung carcinoma cells it can also be secreted by exosomes
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp.
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp.
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp.
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp.
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface of Leishmania spp., no activity in microsomes. Enolase does not contain a detectable secretion signal or membrane anchor region that can explain its membrane localization
-
brenda
additional information
-
in asexual stages, enolase is predominantly present in soluble fraction, while in sexual stages it is mostly associated with particulate fraction
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
-
enolase is found both in the secretome and in association with the surface
-
brenda
additional information
Streptomyces mutans
-
enolase is found both in the secretome and in association with the surface
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
-
enolase 1 and calreticulin siRNA reduce the [Ca2+]i levels, amounts of total TNF-alpha, and the release of TNF-alpha and leukotrienes, all of which are increased in the bone marrow-derived mast cells activated with antigen/antibody reaction
malfunction
-
the down-regulation of enolase selectively increases the susceptibility to phosphomycin
malfunction
-
the down-regulation of enolase selectively increases the susceptibility to phosphomycin
-
metabolism
-
alpha-enolase is involved in glucose metabolism in Alzheimer's disease brain
metabolism
-
enolase 1 is a glycolytic enzyme expressed in most tissues
metabolism
enolase is a key enzyme in the glycolytic pathway
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
Streptomyces mutans
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
Streptomyces pneumoniae
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
in the glycolysis-related energy pathway, enolase might be involved in higher metabolic activity during the day than at night, at least in part, overview
metabolism
-
in tumor cells, ENOA is upregulated and supports anaerobic proliferation, cf. Warburg effect, it is expressed at the cell surface, where it promotes cancer invasion, and is subjected to a specific array of post-translational modifications, namely acetylation, methylation and phosphorylation
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
physiological function
-
alfa-enolase is a fibronectin-binding protein
physiological function
-
alpha-enolase is a glycolytic enzyme that also acts as a surface plasminogen receptor, alpha-enolase elicits a pancreatic ductal adenocarcinoma cell-specific, integrated humoral and cellular response
physiological function
-
ENO-1 binds plasminogen at the cell surface, enhancing local plasmin production, overexpression of ENO-1 in U937 cells increases their migratory and matrix-penetrating capacity
physiological function
-
enolase from Botrytis is cold responsive, influenced by cAMP and acts putatively as a transcriptional regulator of the zinc-C6 protein family and calpain like proteases
physiological function
enolase functions as a protective antigen displayed on the bacterial cell surface
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
-
enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface
physiological function
-
enolase is involved in bacterial adhesion to host epithelial cells
physiological function
-
enolase plays a role in encystation
physiological function
-
glycolytic/gluconeogenesis enzyme, eye lens tau-crystallin protein, plasminogen binding protein, c-Myc binding protein and transcription factor in tumor formationk
physiological function
-
cell surface ENOA is one of the many plasminogen-binding molecules, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256. Binding with ENOA lysyl residues leads to activation of plasminogen to plasmin by the proteolytic action of either tissue-type or urokinase-type plasminogen activators, overview. ENOA takes part, together with urokinase plasminogen activator receptor, integrins and some cytoskeletal proteins, in a multiprotein complex, called metastasome, responsible for adhesion, migration and proliferation in ovarian cancer cells
physiological function
-
enolase 1 and calreticulin are important proteins in regulating the differentiation and functions of bone marrow-derived mast cells
physiological function
enolase acts as a fibronectin binding protein in Paracoccidioides brasiliensis. Association between recombinant PbEno and plasminogen is lysine-dependent and is dependent on cell surface localization of PbENo, since purified rPbEno, in its soluble form, inhibits plasminogen binding to fixed cells, interaction analysis, overview. Exposure of epithelial cells and phagocytes to enolase is associated with an increased expression of surface sites of adhesion. In fact, the association of Paracoccidioides brasiliensis with epithelial cells and phagocytes is increased in the presence of rPbEno
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein, an internal motif, FYDAEKKEY, is responsible for the plasminogen recognition
physiological function
Streptomyces pneumoniae
-
enolase can act as a plasminogen-binding protein, an internal motif, FYDKERKVYD, is responsible for the plasminogen recognition
physiological function
-
enolase is a multifunctional enzyme that is involved in the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate in glycolytic and gluconeogenesis pathways. Csenolase might play key roles in the growth of the parasites. Csenolase is an important glycolytic enzyme required for the development of Clonorchis sinensis
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
-
enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. Enolase can act as a plasminogen-binding protein, an internal motif, AYDAERKMY, is responsible for the plasminogen recognition
physiological function
-
enolase plays an important role in glycolysis. It also binds RNA, overview
physiological function
-
main physiological role of enolase is the reversible conversion of 2-phospho-D-glycerate and to phosphoenolpyruvate within the glycolytic pathway. Enolases play an important role in Cyclamen embryogenesis, overview
physiological function
recombinant SjENO binds to human plasminogen as its receptor
physiological function
the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
the enzyme probably functions in sugar fermentation pathway
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
physiological function
-
enolase is essential for Staphylococcus aureus and involved in the process of bacterial autolysis
physiological function
-
the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
physiological function
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
physiological function
-
the plasminogen-enolase association may play a critical role in the virulence of Salmonella Typhi by causing direct damage to the host cell extracellular matrix
physiological function
enzyme can bind to gen, binding is competitively inhibited by epsilon-aminocaproic acid. Plasminogen bound to Eno can be converted into active plasmin using host-derived activators
physiological function
enzyme can bind to human plasminogen and generate plasmin, activated by a tissue-type plasminogen activator. 6-Aminocaproic acid inhibits the binding of plasminogen to Eno
physiological function
enzyme interacts with human plasminogen and participates in Streptococcus iniae adhesion to and invasion of BHK-21 cells
physiological function
enzyme is involved in type I collagen binding. A strain carrying a null mutation in the EnoA1 gene, binds to immobilized collagen less efficiently than wild-type. EnoA1 binds collagen both under denaturing and native conditions. The region spanning from 73rd to the 140th amino acid residues is involved in collagen binding
physiological function
-
enzyme selectively binds to calcium oxalate monohydrate crystals and interacts directly with Ca2+ and Mg2+. Calcium oxalate monohydrate and Mg2+ competitively bind to alpha-enolase
physiological function
recombinant ENO1 specifically binds to a TTTTCT DNA motif present in the cyst matrix antigen 1 gene promoter
physiological function
recombinant ENO2 specifically binds to a TTTTCT DNA motif present in the cyst matrix antigen 1 gene promoter
physiological function
recombinant enolase EnoA shows a strong plasminogen binding and activating activity in vitro
physiological function
recombinant enolase retains its enzymatic activity and binds to human plasminogen. Binding can be significantly reduced in the presence of epsilon-aminocaproic acid. Eno promotes plasminogen to plasmin conversion in the presence of plasminogen activator
physiological function
-
the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
-
physiological function
-
enzyme is involved in type I collagen binding. A strain carrying a null mutation in the EnoA1 gene, binds to immobilized collagen less efficiently than wild-type. EnoA1 binds collagen both under denaturing and native conditions. The region spanning from 73rd to the 140th amino acid residues is involved in collagen binding
-
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
-
enolase acts as a fibronectin binding protein in Paracoccidioides brasiliensis. Association between recombinant PbEno and plasminogen is lysine-dependent and is dependent on cell surface localization of PbENo, since purified rPbEno, in its soluble form, inhibits plasminogen binding to fixed cells, interaction analysis, overview. Exposure of epithelial cells and phagocytes to enolase is associated with an increased expression of surface sites of adhesion. In fact, the association of Paracoccidioides brasiliensis with epithelial cells and phagocytes is increased in the presence of rPbEno
-
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
-
physiological function
-
enolase plays a role in encystation
-
physiological function
-
alfa-enolase is a fibronectin-binding protein
-
physiological function
-
the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue
-
physiological function
-
recombinant enolase retains its enzymatic activity and binds to human plasminogen. Binding can be significantly reduced in the presence of epsilon-aminocaproic acid. Eno promotes plasminogen to plasmin conversion in the presence of plasminogen activator
-
physiological function
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
-
physiological function
-
enolase is essential for Staphylococcus aureus and involved in the process of bacterial autolysis
-
physiological function
-
enolase functions as a protective antigen displayed on the bacterial cell surface
-
additional information
-
circadian rhythm of enolase in suprachiasmatic nucleus depends on mitochondrial function. Enolase activity, coupled with lactate dehydrogenase, is higher during the light period than that in the dark. However, enolase mRNA, analyzed by RT-PCR, shows higher levels during the dark period than in the light
additional information
-
overexpression of ENOA is associated with tumor development through a process known as aerobic glycolysis or the Warburg effect. ENOA induces autoantibody production and induces a specific immune response in tumors, overview
additional information
-
proteomic analysis and peptide mapping, 2D isoelectric focusing and mass spectrometry, overview
additional information
-
proteomic analysis, peptide mapping, 2D isoelectric focusing, overview
additional information
-
the human muscle-specific enolase is less susceptible to inactivation by reactive aldehydes than the pig enzyme
additional information
-
the human muscle-specific enolase is less susceptible to inactivation by reactive aldehydes than the pig enzyme
additional information
the recombinant enolase is recognized by rabbit sera directed against an antigen preparation from adult worms. 24.28% reduction in the liver egg count and a reduction of 21.45% in the fecal egg count occur in BALB/c mice vaccinated with recombinant SjENO compared with control mice
additional information
-
the recombinant enolase is recognized by rabbit sera directed against an antigen preparation from adult worms. 24.28% reduction in the liver egg count and a reduction of 21.45% in the fecal egg count occur in BALB/c mice vaccinated with recombinant SjENO compared with control mice
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
102800
-
MALDI-TOF, double charged dimer
163000
-
x * 163000, SDS-PAGE
22000
-
monomeric enzyme form, gel filtration, nondenaturing PAGE
25710
-
MALDI-TOF, double charged monomer
300000
-
non-denaturing PAGE
345000
-
gel filtration, high-speed equilibrium sedimentation
350000
-
equilibrium sedimentation
42000
-
8 * 42000, SDS-PAGE
44000
-
2 * 44000, muscle enzyme, SDS-PAGE
452000
-
calculated molecular mass
45545
-
2 * 45545, mass spectrometry and X-ray crystallography
46220
calculated from amino-acid sequence
46461
x * 46461, calculated from amino-acid sequence
46620
determined by mass spectrometry
46672
-
x * 46672, isoform Eno1p, calculated from amino acid sequence
46673
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
46700
x * 48000-52000, SDS-PAGE, x * 46700, calculated
46914
-
x * 46914, calculation from nucleotide sequence
47074
-
x * 47074, calculated from amino acid sequence
47181
-
x * 47181, isoform Err3p, calculated from amino acid sequence
47184
-
x * 47184, isoform Err3p, electrospray ionization mass spectrometry
47196
-
x * 47196, isoform Err2p, calculated from amino acid sequence
47198
-
x * 47198, isoform Err2p, electrospray ionization mass spectrometry
47200
x * 47200, calculated from amino acid sequence
47450
-
x * 47450, sequence calculation and mass spectrometry
47550
deduced from sequence
47600
x * 47600, calculated from amino acid sequence
47790
x * 47790, sequence calculation
48060
-
MALDI-TOF mass spectrometry
51380
-
MALDI-TOF, single charged monomer
53000
-
2 * 53000, liver enzyme, SDS-PAGE
56000
-
x * 56000, SDS-PAGE
61200
-
estimated from SDS-PAGE
63700
-
calculation from sedimentation and diffusion data
82000
-
low speed sedimentation without reaching equilibrium
84970
-
muscle enolase, calculation from amino acid composition
88000
-
sedimentation velocity measurement
89020
-
liver enolase, calculation from amino acid composition
91000
-
liver enzyme, gel filtration
100000
-
gel filtration
100000
-
sucrose density gradient centrifugation
370000
gel filtration
370000
sedimentation velocity analysis
45000
-
SDS-PAGE
45000
-
2 * 45000, SDS-PAGE
45000
-
2 * 45000, SDS-PAGE
45000
x * 45000, SDS-PAGE
45000
-
8 * 45000, SDS-PAGE
46000
-
recombinant enzyme, Western blotting
46000
gel filtration, induced expression of the recombinant protein in Escherichia coli
46000
-
x * 46000, SDS-PAGE
46000
-
2 * 46000, SDS-PAGE
46000
-
x * 46000, enzyme R-NSE, enzyme Y-NSE, SDS-PAGE
46000
-
1 * 46000 + 1 * 49000, enolase II, SDS-PAGE
46000
-
2 * 46000, enolase III, SDS-PAGE
46000
-
2 * 46000, gama,gamma-enolase, SDS-PAGE
46000
-
2 * 46000, liver enzyme, SDS-PAGE
46500
-
x * 46500, SDS-PAGE, H159A and H159G mutants
46500
-
x * 46500, SDS-PAGE, wild type
47000
-
47000
calculated from amino acid sequence
47000
immunoblot analysis
47000
immunoblot analysis
47000
immunoblot analysis
47000
immunoblot analysis
47000
-
x * 47000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
47000
-
x * 47000, SDS-PAGE
47000
x * 47000, SDS-PAGE
47000
x * 47000, SDS-PAGE
47000
-
2 * 47000, SDS-PAGE
47000
-
2 * 47000, SDS-PAGE
47000
-
x * 47000, Y-NSE.H6, SDS-PAGE
47000
x * 47000 about, 2D-gel electrophoresis
47000
-
x * 47000, calculated from amino acid sequence
48000
-
SDS-PAGE
48000
-
enolase 2 and enolase 1, SDS-PAGE
48000
-
x * 48000, SDS-PAGE
48000
-
x * 48000, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE
48000
2 * 48000, SDS-PAGE
48000
-
2 * 48000, recombinant alpha-enolase
48000
-
8 * 48000, a tetramer of dimers, SDS-PAGE
48000
x * 48000, calculated from amino acid sequence
48000
-
x * 48000, MALDI-TOF mass spectrometry
49000
-
gel electrophoresis
49000
-
dimeric enzyme form, gel filtration, native PAGE
49000
-
2 * 49000, enolase I, SDS-PAGE
49000
-
2 * 49000, muscle enzyme, SDS-PAGE
49000
-
1 * 46000 + 1 * 49000, enolase II, SDS-PAGE
49000
-
x * 49000, SDS-PAGE
49000
2 * 49000, gel filtration, the recombinant protein produced in bacteria under native conditions is a dimer
49000
x * 49000, recombinant His-tagged enolase, SDS-PAGE
50000
gel filtration
50000
gel electrophoresis
50000
-
2 * 50000, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
50000
x * 50000, recombinant His-tagged enolase, SDS-PAGE
51000
His-tagged enzyme, SDS-PAGE
51000
-
2 * 51000, SDS-PAGE
51000
-
alpha,gamma, 1 * 51000 + 1 * 52000, brain enolase II, SDS-PAGE
51000
-
alpha,alpha, 2 * 51000, brain enolase I, SDS-PAGE
51400
SDS-PAGE
51500
-
calculated from amino acid sequence
51500
-
beta,beta, 2 * 51500, muscle enolase, SDS-PAGE
52000
-
-
52000
-
2 * 52000, SDS-PAGE
52000
-
2 * 52000, SDS-PAGE
52000
-
alpha,gamma, 1 * 51000 + 1 * 52000, brain enolase II, SDS-PAGE
52000
-
gamma,gamma, 2 * 52000, brain enolase III, SDS-PAGE
52000
x * 52000, His6-tagged enzyme, SDS-PAGE
85000
-
sucrose density gradient ultracentrifugation
85000
-
muscle enzyme, equilibrium sedimentation
90000
-
sedimentation velocity and sedimentation equilibrium experiments
90000
far-UV CD spectroscopy after size-exclusion chromatography
92000
-
gel filtration
92000
-
liver enzyme, equilibrium sedimentation
93000
-
gel filtration
93000
-
muscle enzyme, gel filtration
94000
-
gel filtration
94000
-
native enzyme, gel filtration
96000
-
gel filtration, mutant N207A enzyme
96000
-
gel filtration, wild type enzyme
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monomer
1 * 50000, gel filtration
?
x * 72000, SDS-PAGE, recombinant protein with GST-tag
?
-
x * 72000, SDS-PAGE, recombinant protein with GST-tag
-
?
-
x * 47000, calculated from amino acid sequence
?
-
x * 47000, calculated from amino acid sequence
-
?
-
x * 50000, SDS-PAGE
-
?
x * 49000, recombinant His-tagged enolase, SDS-PAGE
?
-
x * 49000, recombinant His-tagged enolase, SDS-PAGE
-
?
x * 47790, sequence calculation
?
-
x * 163000, SDS-PAGE
-
?
-
x * 45000-66200, recombinant solubilized enzyme, SDS-PAGE
?
-
x * 48000, SDS-PAGE
-
?
-
x * 47074, calculated from amino acid sequence
?
x * 47600, calculated from amino acid sequence
?
-
x * 46000, enzyme R-NSE, enzyme Y-NSE, SDS-PAGE
?
-
x * 47000, Y-NSE.H6, SDS-PAGE
?
-
x * 48000, MALDI-TOF mass spectrometry
?
-
x * 48000, MALDI-TOF mass spectrometry
-
?
-
x * 47450, sequence calculation and mass spectrometry
?
-
x * 46914, calculation from nucleotide sequence
?
x * 47000 about, 2D-gel electrophoresis
?
x * 48000-52000, SDS-PAGE, x * 46700, calculated
?
-
x * 48000-52000, SDS-PAGE, x * 46700, calculated
-
?
-
x * 46500, SDS-PAGE, H159A and H159G mutants
?
-
x * 46500, SDS-PAGE, wild type
?
-
x * 46672, isoform Eno1p, calculated from amino acid sequence
?
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
?
-
x * 47181, isoform Err3p, calculated from amino acid sequence
?
-
x * 47184, isoform Err3p, electrospray ionization mass spectrometry
?
-
x * 47196, isoform Err2p, calculated from amino acid sequence
?
-
x * 47198, isoform Err2p, electrospray ionization mass spectrometry
?
-
x * 46672, isoform Eno1p, calculated from amino acid sequence
-
?
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
-
?
-
x * 47181, isoform Err3p, calculated from amino acid sequence
-
?
-
x * 47184, isoform Err3p, electrospray ionization mass spectrometry
-
?
-
x * 47196, isoform Err2p, calculated from amino acid sequence
-
?
x * 50000, recombinant His-tagged enolase, SDS-PAGE
?
x * 47200, calculated from amino acid sequence
?
-
x * 47000, SDS-PAGE
-
?
-
x * 47200, calculated from amino acid sequence
-
?
x * 47240, calculated from sequence, x * 67000, SDS-PAGE of recombinant protein with His-tag
?
x * 47000, calculated from sequence, x * 66000, SDS-PAGE
?
KX452941
x * 50000, SDS-PAGE
?
x * 46461, calculated from amino-acid sequence
?
x * 48000, calculated from amino acid sequence
?
x * 52000, His6-tagged enzyme, SDS-PAGE
?
-
x * 48000, calculated from amino acid sequence
-
?
-
x * 52000, His6-tagged enzyme, SDS-PAGE
-
dimer
2 * 49000, gel filtration, the recombinant protein produced in bacteria under native conditions is a dimer
dimer
2 * 46000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
-
dimer
-
2 * 51000, SDS-PAGE
dimer
in the crystal structure of 2-phospho-D-glycerate-complexed enzyme, ENO forms an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation, overview
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 45545, mass spectrometry and X-ray crystallography
dimer
-
alpha,gamma, 1 * 51000 + 1 * 52000, brain enolase II, SDS-PAGE
dimer
-
gamma,gamma, 2 * 52000, brain enolase III, SDS-PAGE
dimer
-
alpha,alpha, 2 * 51000, brain enolase I, SDS-PAGE
dimer
-
beta,beta, 2 * 51500, muscle enolase, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 48000, recombinant alpha-enolase
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
the dimeric structure of Pfeno is required for the optimal vacuolar functions
dimer
-
2 * 53000, liver enzyme, SDS-PAGE
dimer
-
2 * 49000, enolase I, SDS-PAGE
dimer
-
2 * 49000, muscle enzyme, SDS-PAGE
dimer
-
1 * 46000 + 1 * 49000, enolase II, SDS-PAGE
dimer
-
2 * 46000, enolase III, SDS-PAGE
dimer
-
2 * 46000, gama,gamma-enolase, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 44000, muscle enzyme, SDS-PAGE
dimer
-
2 * 46000, liver enzyme, SDS-PAGE
heterodimer
-
alpha-gamma-heterodimer
heterodimer
engineered type
homodimer
-
2 * 45000, SDS-PAGE
homodimer
-
2 * 47000, SDS-PAGE
homodimer
-
gel filtration
homodimer
-
2 * 50000, gel filtration
homodimer
-
2 * 50000, gel filtration
-
homodimer
2 * 48000, SDS-PAGE
octamer
-
8 * 42000, SDS-PAGE
octamer
-
8 * 45000, SDS-PAGE
octamer
-
sedimentation velocity analysis
octamer
-
8 * 48000, a tetramer of dimers, SDS-PAGE
additional information
-
the protein contains a potential nuclear localization sequence aa190-199 and several linear B cell epitopes and CTL T cell epitopes, of which the outside epitope aa49-57 and inside epitope aa228-236 are facultative T cell and B cell epitope, and the linear B cell epitope aa206-213 contains the active center site Glu210, suggesting the putative protein is a potential membrane with strong immunogenicity
additional information
composed of a N-terminal alpha,beta domain and a C-terminal domain consisting of eight alpha,alpha barrels, polypeptides packed as tight dimers
additional information
-
the monomer of ENOA consists of a smaller N-terminal domain, residues 1-133, and a larger C-terminal domain, residues 141-431
additional information
extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
additional information
-
extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
additional information
-
extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
-
additional information
dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined
additional information
-
dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined
additional information
subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15°C for 24 h, spectrometrically measured
additional information
-
subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15°C for 24 h, spectrometrically measured
additional information
epitope for plasminogen-binding localized in a surface-exposed loop in each of the monomers of the octameric enolase
additional information
-
epitope for plasminogen-binding localized in a surface-exposed loop in each of the monomers of the octameric enolase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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to 2.0 A resolution, space group R32. Enzyme forms a homodimer with conserved residues in the dimer interface
purified recombinant EhENO with two 2-phospho-D-glycerate substrate molecules bound at the two active sites, the protein solution contains 7.5 mg/ml protein in 100 mM Tris-HCl pH 7.5, 100 mM NaCl, 5 mM MgCl2, sitting-drop vapour-diffusion, 20°C, mixing of equal volumes of precipitant solution, contraining 100 mM Bis-Tris, pH 5.5, 25% w/v PEG 3350, 200 mM ammonium sulfate, and protein solution, X-ray diffractrion structure determination and analysis at 1.9 A resolution, molecular replacement
using the hanging drop method followed by recrystallization under the same conditions, X-ray structure solved by molecular replacement
1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
using the sitting drop method, co-crystallized with Mg2+
-
hanging drop method, 17 A resolution, X-ray coordinates and structure factors determined, complexes with phosphate, with Mg2+, with Mg2+ and HCO3-, with Mg2+ and the alternate substrate 2,3-diketohexane 1-phosphate identified, activated enolase carboxylated on Lys173, conserved Lys98 in the N-terminal domain determined for C1 proton abstraction
1.7 A resolution by multiwavelength anomalous diffraction and molecular replacement techniques
-
asymmetric complex NSE*Mg2SO4/NSE*MgCl, pH 7.0, large orthorhombic plates, structure by molecular replacement
-
at room temperature using the hanging-drop vapour-diffusion method for structure analysis by X-ray diffraction
enolase fluoride/phosphate inhibitory complex and enolase phosphate inhibitory complex
hanging drop vapor diffusion method, using 0.1 M ammonium acetate, 0.1 M bis-tris pH 5.5, 20% (w/v) polyethylene glycol monomethyl ether 2000
hanging drop vapor diffusion method, using 20% (w/v) PEG 550, 100 mM bicine pH 9.0, 100 mM sodium chloride
hanging drop method, from preparations of purified dextransucrase
co-crystallization of the S39A mutant with Mg2+ and phosphonoacetohydroxamate, the active-site flap is opened
-
crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
engineered K345A/N80D/N126D heterodimer in complex with substrate/product, 1.85A resolution, batch method
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate
structure of enolase-Zn2+/Mn2+ complex formation with phosphonoacetohydroxamate solved to 1.54 A resolution by X-ray crystallography, replacement of native Mg2+ ions with Mn2+/Zn2+ introduces only minor atom displacements in the binding site, crystallographic data refined, simulations reveal a model of the enolase active site chosen for the study indicating sites MI and MII either occupied with Mn2+ at site MI and Zn2+ at site MII or vice versa, stereo view of the coordination of the two metal ions in the enolase-inhibitor-complex and of key active site residues presented, rotation patterns shown
2.0 A resolution, molecular replacement, hanging-drop vapor-diffusion
hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 10% (w/v) PEG 20000
to 2.75 A resolution. Residue Glu164 in catalytic loop 2 may account for the comparatively lower activity of this isozyme
hanging drop method, six novel crystal structures with various ligation states and conformations identified, high structural diversity of loops near the catalytic site determined, novel metal-binding site within the catalytic site identified
-
-
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K147A
requires a 10fold greater concentration of protein for observation of enolization
K173A
detectable activity of about 3% of that of wild-type enolase, retains ability to enolize the desthio substrate
K98A
unable to catalyze the enolase reaction
D257K
-
the mutation has no effect on excystation
H389Q/R390S
-
the mutations significantly inhibit excystation
K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K259A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K259A/K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
K259A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
K259A/K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
G157D
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
G376E
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
H159F
-
less than 1% of the activity compared to the wild type
H159N
-
less than 1% of the activity compared to the wild type
K345A/N80D/N126D
heterodimer with one inactive K345A subunit and one active N80D and N126D subunit
N207A
-
50% of the activity compared to the wild type
N80D/N126D
mutant with surface mutations to facilitate ion-exchange chromatographic separation
deltaK433/K434
mutant with different oligomerization state
K433L/K434L
mutant with different oligomerization state
K434L
mutant with different oligomerization state
DELTA434-435
-
mutant with decreased Glu- and Lys-plasminogen-binding activities
F137L/E363G
-
the dimer-dimer interface mutant destabilizes the octameric structure, the double mutant is more easily dissociated in the presence of NaClO4 than is the wild type
K434L/K435L
-
mutant with decreased Glu- and Lys-plasminogen-binding activities
K435L
-
mutant with decreased Glu- and Lys-plasminogen-binding activities
E414L
this mutant has the same activity than the wild-type enzyme
E414L
replacement of an interface glutamate residue with a leucine does not result into dimer dissociation
E168Q
-
the mutant has approximately 0.01% of the activity of native enolase. It binds 3-aminoenolpyruvate-2-phosphate, the 3-amino analogue of the product phosphoenolpyruvate and D-tartronate semialdehyde-2-phosphate, the aldehyde analogue of the substrate 2-phosphoglycerate, the latter two with affinities similar to those of the native enzyme
E168Q
-
severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate
E168Q
the Mg2+ binding site is different compared to the wild type enzyme
E211Q
-
severely depressed activity, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate. Glu211 participates in the second step of the reaction
E211Q
can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate
E211Q
inactive, but properly folded
H159A
-
less than 1% of the activity compared to the wild type
H159A
-
mutation has no effect on conformation or enzyme-ligand complex, but yields an inactive enzyme
K345A
-
severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, fails to catalyze the exchange of the C-2 proton of 2-phospho-D-glycerate with deuterium in D2O, inactive in ionization of tartronate semialdehyde phosphate. Lys345 functions as the base in the ionization of 2-phosphoglycerate
S39A
-
mutant of isoenzyme 1, relative maximal velocity of 0.01% and an activation constant for Mg2+ ca. 10fold higher, compared with the native enzyme
additional information
site-directed mutagenesis of active site residues, spectrophotometric activity assay performed with elevated concentrations of the mutant enzymes
additional information
-
recombinant neuron-specific enolase (R-NSE) has markedly decreased binding affinity to anti-neuron-specific enolase antibodies. Reactivity of modified neuron-specific enolases (Y-NSE with one Tyr residue added at the N-terminal of the recombinant neuron-specific enolase. Y-NSE.H6 with six His residues further added at the C-terminal of recombinant neuron-specific enolase) to the antibody is almost equivalent to that of human brain gamma,gamma-enolase
additional information
-
enolase 1 gene silencing by siRNA leading to reduced the mRNA and protein expressions of surface receptor Fc-RIalpha, surface molecules, such as c-kit, CD40, CD40 ligand and 373 VCAM-1, and also reduced granular tryptase in the culture periods, as well as expressions of enolase 1 and calreticulin. Enolase 1 or calreticulin siRNA transfected-bone marrow-derived mast cells remarkably reduce [Ca2+]i levels compared to wild-type bone marrow-derived mast cells. Both protein siRNA transfected-bone marrow-derived mast cells reduced [Ca2+]i levels more than by individual protein transfection, but does not show additive effect
additional information
immobilization of purified recombinant enolase
additional information
-
immobilization of purified recombinant enolase
additional information
-
immobilization of purified recombinant enolase
-
additional information
-
deletion of a plant like pentapeptide insert 104EWGWS108 in a highly conserved surface loop of the protein results in about 100fold decrease in kcat/Km and causes dissociation of dimeric form into monomers
additional information
-
engineered enolase forms disrupted in catalytic activity retain features to direct mitochondrial import of tRNA
additional information
folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
-
folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
-
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
-
impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
-
replacement of the C-terminal lysine residues by leucine reduces Glu- and Lys-plasminogen-binding properties
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alpha,alpha-enolase and gamma,gamma-enolase
-
ammonium sulfate precipitation and gel filtration
ammonium sulfate precipitation, DEAE Sephadex A-50 gel filtration, Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, DEAE-Sephadex A-50 gel filtration, CM-Sephadex gel filtration, and QAE-Sephadex gel filtration
-
by ion-exchange chromatography and gel filtration
DEAE and carboxymethyl columns, oligonucleotide affinity column
-
enolase 1, enolase II, enolase III
-
extracellular enolase identified from isolates of extracellular dextransucrase from cultures of Leuconostoc mesenteroides, accumulation as small crystals
for localization studies, immunochemistry and confocal microscopy
gel filtration
Plasmodium yoeliie XL17
-
gel filtration of recombinant protein
gel filtration, for in vitro import assays into mitochondria and three-hybrid analysis
-
gel filtration, for localization studies and tubulin-binding kinetics
gel filtration, recombinant enolase of Plasmodium falciparum for vaccination studies in mice
gelatin-agarose affinity column chromatography
glutathione-Sepharose 4B bead chromatography, gel filtration
-
glutathione-Sepharose beads chromatography, gel filtration
-
glutathione-Sepharose-4B chromatography
GSTrap FF column chromatography and Superdex 200 gel filtration
His-Bind column chromatography
His-Trap column chromatography
HiTrap Ni2+-chelating column chromatography and Superdex 75 gel filtration
ion exchange chromatography and gel filtration
MagneHis nickel-conjugated magnetic bead column chromatography, and gel filtration
-
muscle-stage larvae isolated by pepsin-HCl digestion from mice, recombinant enzyme by His Trap chelating column
-
native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
native enzyme partially by preparation of food vacuoles
-
Ni-nitrilotriacetic acid affinity chromatography, eluted with imidazole
-
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography, gel filtration
Ni-NTA resin column chromatography
Ni-NTA Sepharose, ion-exchange chromatography, ammonium sulfate precipitation
-
Ni-NTA-agarose column chromatography, gel filtration
Ni2+-affinity column chromatography
-
Ni2+-charged HiTrap chelating column
nickel affinity column chromatography
nickel-affinity column chromatography and Superdex 200 gel filtration
partial, using ammonium sulfate fractionation and gel filtration chromatography
preparative electrophoresis
-
purification of the wild-type and a mutant enzyme cloned in Escherichia coli using ammonium sulfate precipitation and Sephadex chromatography
Q-Sepharose column chromatography
-
recombinant GST-tagged ENO from Escherichia coli BL21 (DE3) by glutathione affinity chromatography, cleavage of the GST tag, and gel filtration
recombinant His-tagged enolase from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant protein amounts are 10-15% of the total protein, purification from inclusion bodies yields 0.5 mg per liter, allergenic activity of the recombinant protein tested by ELIZA
recombinant protein and natural enolase
recombinant protein, for epitope mapping and identification of plasminogen-binding motifs
recombinant protein, gel filtration
recombinant protein, pET22/14-X vector, His-tag purification, SDS-PAGE
recombinant proteins, SDS-PAGE
recombinant soluble His-tagged enzyme from Escherichia coli by nickel affinity chromatography
to homogeneity, using ammonium sulfate precipitation and DEAE-Sephadex column chromatography
-
using affinity chromatography to isolate a his-tagged recombinant enzyme followed by cleavage of the tag
using affinity chromatography to isolate a his-tagged recombinant enzyme, purification from latex using ammonium sulfate precipitation and gel filtration chromatography
using anion- and cation exchange chromatography
using gel filtration chromatography
-
wild type and several mutant recombinant enzymes using chromatography on Sepharose
-
-
-
His-Trap column chromatography
-
His-Trap column chromatography
native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
-
native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography, gel filtration
-
Ni-NTA column chromatography, gel filtration
-
Ni-NTA column chromatography, gel filtration
-
partial
-
recombinant protein
recombinant protein, gel filtration
recombinant protein, gel filtration
using anion- and cation exchange chromatography
-
using anion- and cation exchange chromatography
-
using anion- and cation exchange chromatography
-
using anion- and cation exchange chromatography
-
using anion- and cation exchange chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ability of Pfeno to complement a mutant Saccharomyces cervisiae strain R11258 deficient in enolase activity. In this strain Tetr-Eno2, the enolase 1 gene is deleted and expression of the enolase 2 gene is under the control of a tetracycline repressible promoter. Pfeno is able to restore all three phenotypic effects fully or partially, i.e. growth retardation, vacuolar fragmentation and altered expression of certain vacuolar proteins, overview
-
cDNA inserted in PGEX-4T-3 expressed in Escherichia coli, glutathione S-transferase fusion protein, protein with 436 amino acid residues, 70-80% sequence similarity to enolases from other organisms, including helminth parasites
clone Eg_PSGRS_13B09, cloning from cDNA library, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) in inclusion bodies
-
co-expression of enolase 1 in bone marrow-derived mast cells with calreticulin
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21 Star(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS using the pRSETA expression vector, recombinant His-tagged protein
expressed in Escherichia coli BL21, pET17b expression vector
expressed in Escherichia coli host strain M15-pREP4, His-tagged protein
expressed in Escherichia coli Rosetta (DE3) cells
-
expressed in Escherichia coli Rosetta (DE3)pLysS cells
-
expressed in Escherichia coli Rosetta cells
-
expressed in Escherichia coli Rosettagami (DE3) cells
expressed in Escherichia coli strains M15 and SG13009 using expression vector pQE30, protein of 431 amino acids identified, homologies to other trematode enolases estimated
expressed in Escherichia coli, expression vector pQE30, His-tagged fusion protein
expressed in Escherichia coli, His-tagged recombinant protein
expressed in Escherichia coli, His-tagging and GST-tagging of recombinant enolase protein
expressed in Escherichia coli, PCR-amplified genomic DNA from Bacillus subtilis strain 168 ligated into pET15b encoding an N-terminal six-His tag vector
expression in Escherichia coli
expression in Escherichia coli of a his-tagged recombinant enzyme
expression in Escherichia coli strain BL21 AI with an N-terminal 10His-tag
expression in Escherichia coli strain DH5alpha with His-tag, recombinant enzyme without enolase activity, gaines activity after cutting off the signal peptide from the full-length protein
-
expression in Escherichia coli strain JM109 with C-terminal His-tag
-
expression in Escherichia coli strain XL1-Blue and BL-21 with N-terminal His-tag
-
expression in Escherichia coli strain XL1Blue as an N-terminal His6-tagged protein
-
expression of GST-tagged ENO in Escherichia coli BL21 (DE3)
expression of GST-tagged enolase in Escherichia coli
expression of His-tagged alpha-enolase in Escherichia coli strain BL21(DE3)
-
expression of His-tagged enolase in Escherichia coli strain BL21
expression of recombinant wild-type and mutant enzymes in Escherichia coli
expression of the mutants E211Q and E168Q in Escherichia coli
expression of the recombinant H159A and H159G mutants in Escherichia coli
-
expression of wild-type and mutant genes in Escherichia coli
-
gene LOS, DNA and amino acid sequence determination and analysis, semi-quantitative RT-PCR expression analysis, overview
identified from cDNA library, expression in Escherichia coli
inserted into pET-3a, expressed in Escherichia coli BL21-DE3, site-directed mutagenesis performed
isolated from a genomic library, over-expressed in Escherichia coli, expression vector pET28a
isolated from cDNA library, expressed in Escherichia coli BL21, expression vector pET22b, 60% sequence similarities to human non-neuronal alpha enolase, conserved residues determined
neuron specific enolase and modified neuron-specific enolases: Y-NSE with one Tyr residue added at the N-terminal of the recombinant neuron-specific enolase
-
over-expression in Escherichia coli strain BL21, expression vector pET3a, His-tagged recombinant protein
-
recombinant enolase, expressed in Escherichia coli BL21-DE3-pLysS strain harbouring the recombinant pET28a plasmid
recombinant protein expressed as a glutathione S-transferase GST::tv-ENO1 fusion protein in Escherichia coli, cleaved using thrombin
-
subcloned in Escherichia coli
the three genes, ENO1, ENO2 and ENO3, encoding for three isoforms of the enzyme, alpha-enolase, gamma-enolase, and beta-enolase, respectively, show high sequence identity
-
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expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli, expression vector pQE30, His-tagged fusion protein
expressed in Escherichia coli, expression vector pQE30, His-tagged fusion protein
Plasmodium yoeliie XL17
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
KX452941
expression in Escherichia coli
expression in Escherichia coli of a his-tagged recombinant enzyme
expression in Escherichia coli of a his-tagged recombinant enzyme
subcloned in Escherichia coli
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subcloned in Escherichia coli
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biofuel production
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
drug development
structure and molecular dynamics applied to design irreversible species-specific inhibitors, parasite-specific lysine residue closely to catalytic site identified
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
Streptomyces mutans
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
Streptomyces pneumoniae
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
drug development
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the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
medicine
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alpha-enolase is a pancreatic ductal adenocarcinoma-associated antigen
medicine
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changes in tumor ENO-1 levels are related to clinical 4-hydroxytamoxifen therapeutic outcome, downregulation of ENO-1 can be utilized as a pharmacological approach for overcoming 4-hydroxytamoxifen resistance in breast cancer therapy
medicine
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salivary neuron specific enolase is an indicator for neuronal damage in patients with ischemic stroke and stroke-prone patients
medicine
the up-regulation of alpha-enolase expression can be a protective mechanism to neutralize oxidative and nitrative stress in diabetes
medicine
the recombinant enzyme protein is a useful antigen in vaccination against adult worms
medicine
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the tegumental membrane protein enolase is a vaccine candidate
medicine
recombinant alpha-enolase can confer effective protection against Streptococcus iniae infection in mice
medicine
vaccine with the enzyme can produce a 36.4% protection rate in vaccinated rabbits against experimental challenges from Taenia pisiformis eggs
molecular biology
alpha-enolase doubles as a surface-displayed plasminogen-binder supporting virulence
molecular biology
influence of enolase on membrane fusion of vacuoles and protein trafficking analyzed
molecular biology
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studies on mitochondrial import machinery of Saccharomyces cerevisiae