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(25R)-3beta-hydroxycholest-5-en-27-oate
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(Z)-3-chloro-2-phosphoenolpyruvate + OH-
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Substrates: wild-type enzyme catalyzes hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3
Products: -
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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
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
3-phospho-D-erythronate
?
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Substrates: -
Products: -
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3-phospho-D-glycerate
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Substrates: -
Products: -
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D-tartronate semialdehyde phosphate
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D-tartronate semialdehyde-2-phosphate
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-
Substrates: substrate analogue that changes its spectrum while bound to the enzyme
Products: -
?
phosphoenolpyruvate
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
additional information
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(25R)-3beta-hydroxycholest-5-en-27-oate

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Substrates: -
Products: -
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(25R)-3beta-hydroxycholest-5-en-27-oate
?
-
Substrates: -
Products: -
?
2,3-diketo-5-methylthiopentane 1-phosphate

2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway
Products: -
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2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
Products: -
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2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway
Products: -
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
Products: -
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway
Products: -
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway, stereochemical course of the reaction catalyzed by enolase determined, C1 proton abstraction
Products: -
?
2,3-diketohexane 1-phosphate

?
Substrates: alternate substrate, C1 proton abstraction
Products: -
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2,3-diketohexane 1-phosphate
?
Substrates: alternate substrate, C1 proton abstraction
Products: -
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2,3-diketohexane 1-phosphate
?
Substrates: alternate substrate, C1 proton abstraction
Products: -
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2-phospho-D-glycerate

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Substrates: the enzyme is a plasminogen binding protein
Products: -
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2-phospho-D-glycerate
?
-
Substrates: 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
Products: -
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2-phospho-D-glycerate
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Substrates: enzyme of glycolysis
Products: -
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2-phospho-D-glycerate
?
-
Substrates: age-related changes in the properties of the enzyme
Products: -
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2-phospho-D-glycerate

phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
?
2-phospho-D-glycerate

phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: the enzyme is involved in the modified Embden-Meyerhof pathway
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: studies on host-trematode relationships, properties of enolase as a host-interacting molecule analyzed
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
C4LXE8
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
C4LXE8
Substrates: substrate binding in pre-catalytic state and during catalysis, recombinant enzyme, overview
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: interaction studies between alpha,alpha enolase and tubulin, co-localization studies with microtubules
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: additional functions apart from glycolytic function of enolase tested
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: kinetic and structural properties of monomeric and dimeric forms of recombinant enolase of Plasmodium falciparum compared
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17
-
Substrates: additional functions apart from glycolytic function of enolase tested, vaccination studies in mice
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17 17XL
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17 17XL
-
Substrates: additional functions apart from glycolytic function of enolase tested, vaccination studies in mice
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: the enzyme probably functions in sugar fermentation pathway
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: in vitro studies on catalytic, divalent cation binding sites
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: separated role of enolase besides function in glycolysis, stimulation of vacuole fusion and involvement in protein trafficking to vacuoles determined
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: influence on exchange of amino acid residues on structure, dissociation and function of enolase analyzed
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: plasminogen-binding activity besides metabolic function
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces mutans
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces pneumoniae
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
KX452941
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: structural analysis
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
D-tartronate semialdehyde phosphate

?
-
Substrates: slowly-reacting strongly bound chromophoric substrate
Products: -
?
D-tartronate semialdehyde phosphate
?
-
Substrates: slowly-reacting strongly bound chromophoric substrate
Products: -
?
phosphoenolpyruvate

2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
?
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate
2-phospho-D-glycerate
-
Substrates: -
Products: -
r
phosphoenolpyruvate + H2O

2-phospho-D-glycerate
-
Substrates: analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin
Products: -
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
Substrates: -
Products: -
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
Substrates: -
Products: -
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
Substrates: -
Products: -
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
Substrates: -
Products: -
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
Substrates: -
Products: -
r
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
Substrates: -
Products: -
r
additional information

?
-
Substrates: enzymes is confirmed by total proteome analysis of glycerol-grown cells
Products: -
?
additional information
?
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
-
Substrates: His-tagged recombinant enolase protein shows a high affinity for human plasminogen
Products: -
?
additional information
?
-
-
Substrates: plasminogen bound to recombinant enolase can be converted to active plasmin
Products: -
?
additional information
?
-
-
Substrates: enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions
Products: -
?
additional information
?
-
-
Substrates: enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions
Products: -
?
additional information
?
-
-
Substrates: plasminogen bound to recombinant enolase can be converted to active plasmin
Products: -
?
additional information
?
-
-
Substrates: enolase shows plasminogen-binding activity
Products: -
?
additional information
?
-
Substrates: the enzyme can bind plasminogen, and lysine analog epsilon-aminocaproic acid significantly inhibits this binding activity, indicating that Dermanyssus gallinae enolase is a receptor of plasminogen
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: the enzyme is a plasminogen-binding protein
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds plasminogen
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds plasminogen
Products: -
?
additional information
?
-
-
Substrates: the enzyme has immunoglobulin E-binding activity
Products: -
-
additional information
?
-
-
Substrates: human immunoglobulin G exhibits stronger binding ability to the enolase C-terminal portion of the enzyme (C1, amino acids 271-432) than pig immunoglobulin G (C2, amino acids 142-271)
Products: -
-
additional information
?
-
-
Substrates: human immunoglobulin G exhibits stronger binding ability to the enolase C-terminal portion of the enzyme (C1, amino acids 271-432) than pig immunoglobulin G (C2, amino acids 142-271)
Products: -
-
additional information
?
-
Substrates: the enzyme binds to plasminogen
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds to plasminogen
Products: -
?
additional information
?
-
Substrates: the enzyme binds to plasminogen
Products: -
?
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
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
phosphoenolpyruvate + H2O
2-phospho-D-glycerate
-
Substrates: analysis of pathogenesis of Bacillus anthracis: binding of human plasminogen and laminin
Products: -
r
additional information
?
-
2,3-diketo-5-methylthiopentane 1-phosphate

2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway
Products: -
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway
Products: -
?
2,3-diketo-5-methylthiopentane 1-phosphate
2-hydroxy-3-keto-5-methylthiopent-1-ene 1-phosphate
Substrates: methionine salvage pathway
Products: -
?
2-phospho-D-glycerate

?
-
Substrates: the enzyme is a plasminogen binding protein
Products: -
?
2-phospho-D-glycerate
?
-
Substrates: 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
Products: -
?
2-phospho-D-glycerate
?
-
Substrates: enzyme of glycolysis
Products: -
?
2-phospho-D-glycerate
?
-
Substrates: age-related changes in the properties of the enzyme
Products: -
?
2-phospho-D-glycerate

phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: the enzyme is involved in the modified Embden-Meyerhof pathway
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
C4LXE8
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Plasmodium yoeliie XL17 17XL
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: the enzyme probably functions in sugar fermentation pathway
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
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r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
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Substrates: analysis of pathogenesis of Streptococcus suis: rSsEno binds to fibronectin and plasminogen
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces mutans
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Streptomyces pneumoniae
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
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2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
Substrates: -
Products: -
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
Products: -
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
Substrates: -
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additional information

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Substrates: plasminogen bound to recombinant enolase can be converted to active plasmin
Products: -
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additional information
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Substrates: plasminogen bound to recombinant enolase can be converted to active plasmin
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additional information
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Substrates: enolase shows plasminogen-binding activity
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
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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-glucose 6-phosphate
21% inhibition at 5 mM (pH 6.8)
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
-
-
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
Sodium fluoride
4% inhibition at 10 mM; 99% inhibition at 10 mM
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
diphosphate

about 20% inhibition at 5 mM
diphosphate
inhibits natural enolase and recombinant protein
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

not inhibited by 3-phosphoglyceric acid, D-glucose 1-phosphate, D-fructose 6-phosphate, L-tyrosine, L-phenylalanine, phosphate, diphosphate and D-glucose 6-phosphate; not inhibited by 3-phosphoglyceric acid, D-glucose 1-phosphate, D-fructose 6-phosphate, and L-phenylalanine
-
additional information
not inhibited by 3-phosphoglyceric acid, D-glucose 1-phosphate, D-fructose 6-phosphate, L-tyrosine, L-phenylalanine, phosphate, diphosphate and D-glucose 6-phosphate; not inhibited by 3-phosphoglyceric acid, D-glucose 1-phosphate, D-fructose 6-phosphate, and L-phenylalanine
-
additional information
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the muscle-specific enolase is used as a model enzyme for inhibition analysis by acrolein, 4-hydroxy-2-nonenal, and trans-2-nonenal, incubation for 1-24 h at 25°C, 37°C, and 45°C, overview. The compounds show inhibition effectivity in the following descending order: inhibition degree of enolase activity occurred in following order: 4-hydroxy-2-nonenal, acrolein, methylglyoxal, trans-2-nonenal, overview
-
additional information
antibodies against enolase inhibits up to 60% of plasminogen binding
-
additional information
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antibodies against enolase inhibits up to 60% of plasminogen binding
-
additional information
recombinant enolase inhibits activity of purified dextransucrase
-
additional information
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recombinant enolase inhibits activity of purified dextransucrase
-
additional information
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no inhibition by NEM and iodoacetate
-
additional information
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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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0.107
-
pH 7.5, 37°C, activity in undialyzed cell extracts
0.41
-
crude extract, at pH 7.8
0.79
-
substrate: 2-phospho-D-glycerate, 50°C, pH not specified in the publication, enzyme from starch-grown cells
0.9
-
crude extract, at pH 6.8
1.1
-
H159N mutant, pH 7.8, 21ºC
1.9
-
H159F mutant, pH 7.8, 21ºC
10050
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Zn2+
11.29
substrate phosphoenolpyruvate, 22°C, pH not specified in the publication
111
room temperature, pH 7.5, MgCl2, KCl, 2-phosphoglyceric acid
1118
-
dimeric enzyme form
15.87
purified recombinant enzyme, substrate phosphoenolpyruvate, pH 7.4, 20°C
197.4
-
plastidic isoenzyme
23.2
-
SPM2, 0.25% Triton X-100
248
-
N207A mutant, pH 7.8, 21ºC
252.4
-
cytosolic isoenzyme
260
-
pH 8.1, room temperature
3.3
-
H159A mutant, pH 7.8, 21ºC
30
-
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
-
after 76.1fold purification, at pH 7.8
35.81
purified recombinant enzyme, substrate 2-phospho-D-glycerate, pH 7.4, 20°C
3909
purifed recombinant enzyme, pH 8.5, 37°C, no metal ion added
442
-
wild type, pH 7.8, 21ºC
60.72
pH not specified in the publication, temperature not specified in the publication
67
recombinant wild-type enzyme, pH 7.1, 25ºC
67.4
-
enolase from synaptosomal cytoplasm
700
-
pH 7.6, temperature not specified in the publication
75
-
after 83fold purification, at pH 6.8
77
recombinant E414L mutant, pH 7.1, 25ºC
9091
purifed recombinant enzyme, pH 8.5, 37°C, 10 mM Mg2+
918
-
monomeric enzyme form
51

-
-
60 - 70

-
pH 7.4
87

-
muscle enolase
additional information

functional activity of recombinant protein shown, immunogenicity determined by ELISA and Western Blot using different sera, natural infection of humans by Anisakis simplex larvae lacks sufficient antigenic stimuli
additional information
-
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
-
-
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
-
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
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
activity of recombinant protein spectrophotometrically measured by conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, substrate concentrations of 3 mM
additional information
-
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
-
31.2 nmol 2-PGA converted/min/36nM enolase
additional information
recombinant enolase protein of Plasmodium falciparum can protect mice against malaria, assay described
additional information
-
recombinant enolase protein of Plasmodium falciparum can protect mice against malaria, assay described
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
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
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
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
-
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
-
purified recombinant enolase has plasminogen binding activity, analyzed by flow cytometry
additional information
-
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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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
-
inhibiting glycolysis activity of the enzyme using 2-deoxy-D-glucose treatment significantly reduces the stemness of gastric cancer cells
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 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
-
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 1 is a glycolytic enzyme expressed in most tissues
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
-
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
-
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
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
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
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

-
enolase plays a role in encystation
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
enolase functions as a protective antigen displayed on the bacterial cell surface
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
-
alfa-enolase is a fibronectin-binding protein
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 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 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
-
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 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
-
enolase 1 and calreticulin are important proteins in regulating the differentiation and functions of bone marrow-derived mast cells
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
-
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
-
enolase plays an important role in glycolysis. It also binds RNA, overview
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 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 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 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
recombinant SjENO binds to human plasminogen as its receptor
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
Streptomyces pneumoniae
-
enolase can act as a plasminogen-binding protein, an internal motif, FYDKERKVYD, is responsible for the plasminogen recognition
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
-
the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
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 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
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
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
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
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
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
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
enzyme interacts with human plasminogen and participates in Streptococcus iniae adhesion to and invasion of BHK-21 cells
physiological function
-
enolase 1 can improve the stemness of gastric cancer stem cells by enhancing the cells' glycolysis
physiological function
-
enolase Pla a 6 is an allergen in the Platanus acerifolia pollen
physiological function
-
the enzyme serves as an anchor to bind to the cell surface and displays beta-galactosidase on the 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 plays a role in encystation
-
physiological function
-
alfa-enolase is a fibronectin-binding protein
-
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 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
-
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
-
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 plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
-
physiological function
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
-
physiological function
-
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
-
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 serves as an anchor to bind to the cell surface and displays beta-galactosidase on the surface
-
additional information

-
proteomic analysis, peptide mapping, 2D isoelectric focusing, overview
additional information
-
proteomic analysis and peptide mapping, 2D isoelectric focusing and mass spectrometry, overview
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
-
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
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
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
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
-
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

-
SDS-PAGE
47000
immunoblot analysis
47000
immunoblot analysis
47000
immunoblot analysis
47000
immunoblot analysis
47000
calculated from amino acid sequence
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

-
dimeric enzyme form, gel filtration, native PAGE
49000
-
gel electrophoresis
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

-
SDS-PAGE
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

-
MALDI-TOF
51500

-
calculated from amino acid sequence
51500
-
beta,beta, 2 * 51500, muscle enolase, SDS-PAGE
52000

2D-PAGE
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

-
muscle enzyme, equilibrium sedimentation
85000
-
sucrose density gradient ultracentrifugation
90000

-
sedimentation velocity and sedimentation equilibrium experiments
90000
far-UV CD spectroscopy after size-exclusion chromatography
92000

-
liver enzyme, equilibrium sedimentation
93000

-
gel filtration
93000
-
muscle enzyme, gel filtration
94000

-
gel filtration
94000
-
native enzyme, gel filtration
96000

-
gel filtration, wild type enzyme
96000
-
gel filtration, mutant N207A enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
1 * 50000, gel filtration
?

x * 72000, SDS-PAGE, recombinant protein with GST-tag
?
-
x * 72000, SDS-PAGE, recombinant protein with GST-tag
-
?
-
x * 46400, calculated from amino acid sequence
?
-
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 * 48900, His6-tagged isoform ENO2, calculated from amino acid sequence
?
x * 48000, His6-tagged isoform ENO2, SDS-PAGE
?
x * 46700, His6-tagged isoform ENO1, calculated from amino acid sequence
?
x * 52000, His6-tagged isoform ENO1, SDS-PAGE
?
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, wild type
?
-
x * 46500, SDS-PAGE, H159A and H159G mutants
?
-
x * 46672, isoform Eno1p, calculated from amino acid sequence
?
-
x * 47196, isoform Err2p, calculated from amino acid sequence
?
-
x * 47181, isoform Err3p, calculated from amino acid sequence
?
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
?
-
x * 47198, isoform Err2p, electrospray ionization mass spectrometry
?
-
x * 47184, isoform Err3p, electrospray ionization mass spectrometry
?
-
x * 46672, isoform Eno1p, calculated from amino acid sequence
-
?
-
x * 47196, isoform Err2p, calculated from amino acid sequence
-
?
-
x * 47181, isoform Err3p, calculated from amino acid sequence
-
?
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
-
?
-
x * 47198, isoform Err2p, electrospray ionization mass spectrometry
-
?
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 * 47095, calculated from amino acid sequence
?
-
x * 47095, calculated from amino acid sequence
-
?
-
x * 50000, SDS-PAGE
-
?
-
x * 66000, green fluorescent protein-tagged enzyme, SDS-PAGE
?
-
x * 66000, green fluorescent protein-tagged enzyme, SDS-PAGE
-
?
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
C4LXE8
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 * 50000, SDS-PAGE
dimer
-
2 * 48000, recombinant alpha-enolase
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 47000, 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 * 52000, SDS-PAGE
dimer
-
2 * 45000, 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
-
2 * 50000, gel filtration
homodimer
-
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
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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
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extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
additional information
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extracellular enolase predicted as octamer, with two of its subunits defining the asymmetric unit of the crystal
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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
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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
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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
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epitope for plasminogen-binding localized in a surface-exposed loop in each of the monomers of the octameric enolase
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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
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the mutation has no effect on excystation
H389Q/R390S
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the mutations significantly inhibit excystation
K255A
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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
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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
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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
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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
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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K259A K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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K259A/K422A K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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K422A K255A
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while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
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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
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less than 1% of the activity compared to the wild type
H159N
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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
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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
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mutant with decreased Glu- and Lys-plasminogen-binding activities
F137L/E363G
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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
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mutant with decreased Glu- and Lys-plasminogen-binding activities
K435L
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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

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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
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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

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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

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less than 1% of the activity compared to the wild type
H159A
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mutation has no effect on conformation or enzyme-ligand complex, but yields an inactive enzyme
K345A

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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

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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
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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
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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
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immobilization of purified recombinant enolase
additional information
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immobilization of purified recombinant enolase
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additional information
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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
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engineered enolase forms disrupted in catalytic activity retain features to direct mitochondrial import of tRNA
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
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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
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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
folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
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folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
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replacement of the C-terminal lysine residues by leucine reduces Glu- and Lys-plasminogen-binding properties
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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
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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
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co-expression of enolase 1 in bone marrow-derived mast cells with calreticulin
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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
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expressed in Escherichia coli Rosetta (DE3)pLysS cells
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expressed in Escherichia coli Rosetta cells
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expressed in Escherichia coli Rosetta-gami 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 XL1-Blue cells and Nicotiana benthamiana
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
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expression in Escherichia coli strain JM109 with C-terminal His-tag
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expression in Escherichia coli strain XL1-Blue and BL-21 with N-terminal His-tag
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expression in Escherichia coli strain XL1Blue as an N-terminal His6-tagged protein
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expression of GST-tagged ENO in Escherichia coli BL21 (DE3)
C4LXE8
expression of GST-tagged enolase in Escherichia coli
expression of His-tagged alpha-enolase in Escherichia coli strain BL21(DE3)
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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
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expression of wild-type and mutant genes in Escherichia coli
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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
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over-expression in Escherichia coli strain BL21, expression vector pET3a, His-tagged recombinant protein
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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
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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
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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
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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
expressed in Escherichia coli BL21(DE3) 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
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
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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, 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

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 of a his-tagged recombinant enzyme

expression in Escherichia coli of a his-tagged recombinant enzyme
subcloned in Escherichia coli

subcloned in Escherichia coli
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