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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Plasmodium falciparum and UniProt Accession Q8IJN7
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4.2.1.11 phosphopyruvate hydrataseIUBMB Comments
Also acts on 3-phospho-D-erythronate.
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Word Map
- 4.2.1.11
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chromogranin
- glial
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neuroendocrine
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synaptophysin
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fibrillary
- vimentin
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cytokeratins
- neurofilament
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- neoplasm
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carcinoembryonic
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resect
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immunocytochemical
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cerebrospinal
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neuroectodermal
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postoperative
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primitive
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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
- paragangliomas
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epithelioid
-
dense-core
-
merkel
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argyrophilic
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glasgow
- gastrin
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neuron-like
- comatose
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polypoid
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fibrovascular
- bombesin
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myxoid
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out-of-hospital
- drug development
- biofuel production
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuron-specific enolase, enolase, neuron specific enolase, alpha-enolase, gamma-enolase, enolase 1, beta-enolase, yeast enolase, enolase 2, eno-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-phospho-D-glycerate hydro-lyase
-
-
-
-
2-phosphoglycerate dehydratase
-
-
-
-
2-phosphoglycerate enolase
-
-
-
-
2-phosphoglyceric dehydratase
-
-
-
-
alpha,alpha-enolase
-
-
-
-
Alt a XI
-
-
-
-
beta,beta-enolase
-
-
-
-
Cla h VI
-
-
-
-
enolase
gamma,gamma-enolase
-
-
-
-
gamma-enolase
-
-
-
-
HLE1
-
-
-
-
hydratase, phosphoenolpyruvate
-
-
-
-
Laminin binding protein
-
-
-
-
Major allergen Alt a 11
-
-
-
-
MSE
-
-
-
-
Neural enolase
-
-
-
-
neuron-specific enolase
-
-
-
-
NNE
-
-
-
-
Non-neural enolase
-
-
-
-
NSE
-
-
-
-
OSE1
-
-
-
-
phosphoenolpyruvate hydratase
-
-
-
-
Phosphopyruvate hydratase
-
-
-
-
R-NSE
-
-
-
-
Skeletal muscle enolase
-
-
-
-
Tau-crystallin
-
-
-
-
enolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Also acts on 3-phospho-D-erythronate.
CAS REGISTRY NUMBER
COMMENTARY
9014-08-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
additional functions apart from glycolytic function of enolase tested
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
kinetic and structural properties of monomeric and dimeric forms of recombinant enolase of Plasmodium falciparum compared
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KBr
dimeric form 10-20% activated, monomeric form strongly inhibited
KCl
dimeric form 10-20% activated, monomeric form strongly inhibited
Mg2+
Mg2+
protects enolases of yeast and of rabbit muscle but not of Plasmodium falciparum from dissociation in presence of imidazol
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
inhibits dimeric and monomeric forms of the enzyme, inhibition stronger for the monomeric form
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
disruption of subunit-subunit interactions declines enzyme activity 3fold
-
additional information
additional information
-
disruption of subunit-subunit interactions declines enzyme activity 3fold
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
pH-dependent dissociation reveals that protonation of groups at the intersubunit interface is responsible for dissociation
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
human serum samples collected from residents living in areas of Eastern India, where Plasmodium falciparum is endemic, 96% reactivity of the recombinant enolase r-Pfren determined
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
surface-localization on merozoites determined by indirect immunofluorescence assay
-
secreted enzyme associated to the external surface of the parasite
-
secreted enzyme associated to the external surface of the parasite
-
additional information
-
in asexual stages, enolase is predominantly present in soluble fraction, while in sexual stages it is mostly associated with particulate fraction
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
enolase can act as a plasminogen-binding protein
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
the dimeric structure of Pfeno is required for the optimal vacuolar functions
homodimer
additional information
additional information
dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined
additional information
-
dissociation studies of homodimeric enolases into their active monomeric forms, analysis of intersubunit interactions and influence on catalytic and structural stability, properties of monomeric enolase determined
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E414L
replacement of an interface glutamate residue with a leucine does not result into dimer dissociation
additional information
-
deletion of a plant like pentapeptide insert 104EWGWS108 in a highly conserved surface loop of the protein results in about 100fold decrease in kcat/Km and causes dissociation of dimeric form into monomers
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44.7
-
dimeric recombinant enolase shows two transitions which corresponds to dissociation of dimer in to monomer (Tm of 44.7°C)
58.1
-
dimeric recombinant enolase shows two transitions which corresponds to unfolding of monomer (Tm of 58.1°C)
additional information
additional information
thermal stability different in monomeric and dimeric forms, the dimeric form is stable at 37°C and shows 20-25% inactivation at 50°C, the monomeric form is to 80% inactivated at 37°C after 2h and completely inactivated at 50°C
additional information
-
thermal stability different in monomeric and dimeric forms, the dimeric form is stable at 37°C and shows 20-25% inactivation at 50°C, the monomeric form is to 80% inactivated at 37°C after 2h and completely inactivated at 50°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, recombinant enolase of Plasmodium falciparum for vaccination studies in mice
Ni-nitrilotriacetic acid affinity chromatography, eluted with imidazole
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, expression vector pQE30, His-tagged fusion protein
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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expression in Escherichia coli strain XL1Blue as an N-terminal His6-tagged protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the glycolytic/gluconeogenic enzyme enolase is a candidate target for antiparasite drug design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pal-Bhowmick, I.; Sadagopan, K.; Vora, H.K.; Sehgal, A.; Sharma, S.; Jarori, G.K.
Cloning, over-expression, purification and characterization of Plasmodium falciparum enolase
Eur. J. Biochem.
271
4845-4854
2004
Plasmodium falciparum, Plasmodium falciparum NF54
Pal-Bhowmick, I.; Krishnan, S.; Jarori, G.K.
Differential susceptibility of Plasmodium falciparum versus yeast and mammalian enolases to dissociation into active monomers
FEBS J.
274
1932-1945
2007
Plasmodium falciparum (Q27727), Plasmodium falciparum
Pal-Bhowmick, I.; Mehta, M.; Coppens, I.; Sharma, S.; Jarori, G.K.
Protective properties and surface localization of Plasmodium falciparum enolase
Infect. Immun.
75
5500-5508
2007
Plasmodium yoeliie XL17, Plasmodium falciparum (Q8IJN7), Plasmodium falciparum, Plasmodium yoeliie XL17 17XL
Vora, H.K.; Shaik, F.R.; Pal-Bhowmick, I.; Mout, R.; Jarori, G.K.
Effect of deletion of a plant like pentapeptide insert on kinetic, structural and immunological properties of enolase from Plasmodium falciparum
Arch. Biochem. Biophys.
485
128-138
2009
Plasmodium falciparum
Bhowmick, I.P.; Kumar, N.; Sharma, S.; Coppens, I.; Jarori, G.K.
Plasmodium falciparum enolase: stage-specific expression and sub-cellular localization
Malar. J.
8
179
2009
Plasmodium falciparum
Avilan, L.; Gualdron-Lopez, M.; Quinones, W.; Gonzalez-Gonzalez, L.; Hannaert, V.; Michels, P.A.; Concepcion, J.L.
Enolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target
Enzyme Res.
2011
932549
2011
Aeromonas hydrophila, Candida albicans, Eimeria tenella, Fasciola hepatica, Giardia intestinalis, Lactobacillus crispatus, Leishmania braziliensis, Leishmania donovani, Leishmania infantum, Leishmania major, Leishmania mexicana, Plasmodium falciparum, Schistosoma japonicum, Streptococcus pyogenes, Streptomyces mutans, Streptomyces pneumoniae, Trichomonas vaginalis, Trypanosoma brucei, Trypanosoma cruzi, Schistosoma bovis, Leishmania chagasi, Echinostoma caproni
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