4.2.1.11: phosphopyruvate hydratase
This is an abbreviated version!
For detailed information about phosphopyruvate hydratase, go to the full flat file.
Word Map on EC 4.2.1.11
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4.2.1.11
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chromogranin
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glial
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neuroendocrine
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synaptophysin
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fibrillary
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vimentin
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cytokeratins
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neurofilament
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nerve
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neoplasm
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cerebral
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tumour
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carcinoembryonic
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actin
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metastases
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adenocarcinoma
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resect
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desmin
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woman
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immunocytochemical
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neuroblastoma
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cerebrospinal
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csf
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carcinoid
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neuroectodermal
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somatostatin
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postoperative
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primitive
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calcitonin
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keratin
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spindle
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neurosecretory
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pleomorphic
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small-cell
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polygonal
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histogenesis
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paragangliomas
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epithelioid
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dense-core
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merkel
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argyrophilic
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glasgow
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gastrin
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neuron-like
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comatose
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polypoid
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fibrovascular
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bombesin
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myxoid
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out-of-hospital
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drug development
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biofuel production
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medicine
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molecular biology
- 4.2.1.11
-
chromogranin
- glial
-
neuroendocrine
-
synaptophysin
-
fibrillary
- vimentin
-
cytokeratins
- neurofilament
- nerve
- neoplasm
- cerebral
- tumour
-
carcinoembryonic
- actin
- metastases
- adenocarcinoma
-
resect
- desmin
- woman
-
immunocytochemical
- neuroblastoma
-
cerebrospinal
- csf
- carcinoid
-
neuroectodermal
- somatostatin
-
postoperative
-
primitive
- calcitonin
- keratin
-
spindle
-
neurosecretory
-
pleomorphic
-
small-cell
-
polygonal
-
histogenesis
- paragangliomas
-
epithelioid
-
dense-core
-
merkel
-
argyrophilic
-
glasgow
- gastrin
-
neuron-like
- comatose
-
polypoid
-
fibrovascular
- bombesin
-
myxoid
-
out-of-hospital
- drug development
- biofuel production
- medicine
- molecular biology
Reaction
Synonyms
14-3-2 protein, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydrolase, 2-phospho-D-glycerate hydrolyase, 2-phospho-D-glyceratehydrolyase, 2-phosphoglycerate dehydratase, 2-phosphoglycerate enolase, 2-phosphoglycerate hydrolase, 2-phosphoglycerate hydrolyase, 2-phosphoglyceric dehydratase, 2-phosphopyruvate hydrolyase, alpha,alpha-enolase, alpha-enolase, alpha-enolase 1, alpha-enolase 2, Alt a XI, beta,beta-enolase, beta-enolase, Cla h VI, Csenolase, cytotoxin B, EhENO, ENO, ENO-1, Eno-alpha, ENO-S, ENO1, Eno1p, Eno2, ENOA, EnoA I, EnoA1, ENOL, Enol-1, enolase, enolase 1, enolase 2, enolase alpha, enolase gamma, enolase S, enolase-1, enolase-alpha, enolase-beta, Enolase-phosphatase E1, enolase2p, Err2p, Err3p, gamma,gamma-enolase, gamma-enolase, hENO1, HLE1, human alpha-enolase, human neuron-specific enolase, hydratase, phosphoenolpyruvate, Laminin binding protein, Major allergen Alt a 11, MASA, MSE, Neural enolase, neuron specific enolase, neuron-specific enolase, neuronal enolase, NNE, Non-neural enolase, NSE, OSE1, p45, P46, Pfen, Pfeno, phosphoenolpyruvate enolase, phosphoenolpyruvate hydratase, Phosphopyruvate hydratase, plasminogen-binding alpha-enolase, R-NSE, r-Pfen, rBaEn, rSsEno, SEN, SjENO, Skeletal muscle enolase, SPM2, SsEno, SSO0913, streptococcal surface enolase, Tau-crystallin, tv-ENO1, tv-rENO1, XEP, yeast enolase
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4.2.1.11 phosphopyruvate hydrataseAdvanced search results
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results (Inhibitors
Inhibitors on EC 4.2.1.11 - phosphopyruvate hydratase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
cumene hydroperoxide
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1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h
D-glycerate-2-phosphate
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mixed-type inhibition in the binding of D-glycerate-2-phosphate and D-phosphoglycerate mutase to the D-glycerate-2-phosphate binding site on the enolase in absence of D-glycerate-2,3-diphosphate, inhibition is almost fully reverted by D-glycerate-2,3-diphosphate
p19ras
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when full-length p19ras and C-terminal region are bound to NSE, it inhibits the enzymatic activity of NSE, p19ras interacts with enolase alpha and represses its enzymatic activity in vitro
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peracetic acid
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1% residual activity after treatment with 4 mM peracetic acid at 25°C and pH 7 for 15 min
tert-butyl hydroperoxide
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1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50°C and pH 7 for 3 h
2-phosphoglycerate
presence of 0.8 mM 2-phosphoglycerate abolished the binding of beta,beta-enolase to tubulin, kinetics shown
F-
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noncompetitive in the presence of phosphate, competitive in the absence of phosphate
F-
non-competitive inhibition without phosphate and in presence of 1 mM phosphate, competitive inhibition in presence of 20 mM phosphate
F-
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in absence of phosphate noncompetitive inhibition up to 10 mM F-, competitive inhibition in presence of 0.5 mM phosphate
fluoride
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the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
fluoride
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the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
methylglyoxal
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incubation of0.015 mM enzyme with 2 mM, 3.1 mM and 4.34 mM methylglyoxal in 100 mM phosphate buffer pH 7.4 for 3 h causes the loss a 32%, 55% and 82% of initial specific activity, respectively. Inhibition of enolase by methylglyoxal and formation of enolase-derived glycation products arises more effectively in slight alkaline conditions and in the presence of inorganic phosphate
Mg2+
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Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
Mg2+
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inhibitor above 1 mM, N207A, H159A, H159N and H159F mutants are stimulated at this concentration
Mg2+
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Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
NaCl
inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form
NaClO4
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inactivation is due to dissociation of the enolase into inactive monomers, 2-phospho-D-glycerate prevents this inactivation
NaClO4
E414L mutant is more sensitive to inactivation than the wild-type enzyme
NaClO4
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enolase at 19.4 mM after incubation in 0.2 M NaClO4, has 32% of its original activity and is 21% octameric. Following a 24 h dialysis against buffer, the protein is 77% octameric and has 74% of its original activity
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
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at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
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at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
phosphate
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competitive inhibition at 2-4 mM phosphate with respect to 2-phosphoglycerate becomes noncompetitive in presence of 20-40 mM phosphate
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
additional information
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the muscle-specific enolase is used as a model enzyme for inhibition analysis by acrolein, 4-hydroxy-2-nonenal, and trans-2-nonenal, incubation for 1-24 h at 25°C, 37°C, and 45°C, overview. The compounds show inhibition effectivity in the following descending order: inhibition degree of enolase activity occurred in following order: 4-hydroxy-2-nonenal, acrolein, methylglyoxal, trans-2-nonenal, overview
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additional information
antibodies against enolase inhibits up to 60% of plasminogen binding
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additional information
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antibodies against enolase inhibits up to 60% of plasminogen binding
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additional information
recombinant enolase inhibits activity of purified dextransucrase
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additional information
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recombinant enolase inhibits activity of purified dextransucrase
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additional information
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inhibition of enolase by fluoride in combination with phosphate can influence glycolysis and so reduce acid production of even growth rate, thereby leading to potential anticariogenic effects
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additional information
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the muscle-specific enolase is used as a model enzyme for inhibition analysis by acrolein, 4-hydroxy-2-nonenal, and trans-2-nonenal, incubation for 1-24 h at 25°C, 37°C, and 45°C, overview. The compounds show inhibition effectivity in the following descending order: inhibition degree of enolase activity occurred in following order: 4-hydroxy-2-nonenal, acrolein, methylglyoxal, trans-2-nonenal, overview
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