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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Eimeria tenella and UniProt Accession Q967Y8

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.11 phosphopyruvate hydratase
IUBMB Comments
Also acts on 3-phospho-D-erythronate.
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This record set is specific for:
Eimeria tenella
UNIPROT: Q967Y8
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The taxonomic range for the selected organisms is: Eimeria tenella
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, laminin binding protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Also acts on 3-phospho-D-erythronate.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-08-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isolated after infection of 2-week-old White Leghorn PA12 chickens for 68 h, protein but not cDNA detected in the sporozoite stage, expression enhanced during the first schizogony
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
partly localized inside the nucleus of sporozoites and schizonts, partly secreted, apex of the first generation of merozoites, relocalization inside sporozoites observed
Manually annotated by BRENDA team
-
associated to the external surface of the parasite
Manually annotated by BRENDA team
-
secreted enzyme
-
Manually annotated by BRENDA team
additional information
-
enolase is found both in the secretome and in association with the surface
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENO_EIMTE
445
0
47975
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
gel electrophoresis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, pET22/14-X vector, His-tag purification, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
identified from cDNA library, expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Labbe, M.; Peroval, M.; Bourdieu, C.; Girard-Misguich, F.; Pery, P.
Eimeria tenella enolase and pyruvate kinase: a likely role in glycolysis and in others functions
Int. J. Parasitol.
36
1443-1452
2006
Eimeria tenella (Q967Y8), Eimeria tenella, Eimeria tenella PaPt36 (Q967Y8)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team