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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Mus musculus and UniProt Accession P17182
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4.2.1.11 phosphopyruvate hydrataseIUBMB Comments
Also acts on 3-phospho-D-erythronate.
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- 4.2.1.11
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chromogranin
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neuroendocrine
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synaptophysin
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fibrillary
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cytokeratins
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resect
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immunocytochemical
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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
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merkel
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argyrophilic
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glasgow
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neuron-like
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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
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The taxonomic range for the selected organisms is: Mus musculus
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, laminin binding protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-phospho-D-glycerate hydro-lyase
-
-
-
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2-phosphoglycerate dehydratase
-
-
-
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2-phosphoglycerate enolase
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-
-
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2-phosphoglyceric dehydratase
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-
-
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alpha,alpha-enolase
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-
-
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Alt a XI
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-
-
-
beta,beta-enolase
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-
-
-
Cla h VI
-
-
-
-
enolase
gamma,gamma-enolase
-
-
-
-
gamma-enolase
-
-
-
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HLE1
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-
-
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hydratase, phosphoenolpyruvate
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-
-
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Laminin binding protein
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-
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Major allergen Alt a 11
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-
-
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MSE
-
-
-
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Neural enolase
-
-
-
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neuron-specific enolase
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-
-
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NNE
-
-
-
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Non-neural enolase
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-
-
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NSE
-
-
-
-
OSE1
-
-
-
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phosphoenolpyruvate hydratase
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-
-
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Phosphopyruvate hydratase
-
-
-
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R-NSE
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-
-
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Skeletal muscle enolase
-
-
-
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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
?
-
beta,beta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), beta,beta-enolase binds with high affinity sarcomeric troponin but not actin and tropomyosin
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
interaction studies between alpha,alpha enolase and tubulin, co-localization studies with microtubules
-
-
?
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
?
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enolase 1 is a metalloenzyme with an absolute requirement for divalent metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-phosphoglycerate
presence of 0.8 mM 2-phosphoglycerate abolished the binding of beta,beta-enolase to tubulin, kinetics shown
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
satellite cell differentiation, alpha,alpha-enolase highly expressed during early ontogenesis, concentration of alpha,alpha-enolase in skeletal muscle varies from 0.1 mM to 0.01 mM until differentiation, binding affinity to tubulin is about 0.2 microM, alpha,beta heteroassociation with tubulin in muscle under physiological conditions
alpha,beta heterodimer and beta,beta homodimer in striated muscle, interaction with tubulin during differentiation of muscle satellite cells but not in undifferentiated myoblasts, immobilized beta,beta-enolase interacts with tubulin in vitro
additional information
additional information
-
the embryonic alpha,alpha isoform remains distributed in many adult cell types, wheras a transition towards beta,beta-isoform and gamma,gamma-isoform occurs in striated muscle cells and neurons respectively
additional information
-
enolase 1 is a glycolytic enzyme expressed in most tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
cytosolic fractions of myoblasts and myotubes, microtubule-association of alpha,alpha-enolase in undifferentiated myoblasts and in myotubes, also nuclear localization in myoblasts but not in myotubes determined, role of enolases in cytoskeletal dynamics during myoblast differentiation assumed
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
enolase 1 and calreticulin are important proteins in regulating the differentiation and functions of bone marrow-derived mast cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ENOA_MOUSE
434
0
47141
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enolase 1 gene silencing by siRNA leading to reduced the mRNA and protein expressions of surface receptor Fc-RIalpha, surface molecules, such as c-kit, CD40, CD40 ligand and 373 VCAM-1, and also reduced granular tryptase in the culture periods, as well as expressions of enolase 1 and calreticulin. Enolase 1 or calreticulin siRNA transfected-bone marrow-derived mast cells remarkably reduce [Ca2+]i levels compared to wild-type bone marrow-derived mast cells. Both protein siRNA transfected-bone marrow-derived mast cells reduced [Ca2+]i levels more than by individual protein transfection, but does not show additive effect
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-74°C, pH 7.0, stable for up to 10 months, provided that multiple freezing and thawing steps are avoided
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, for localization studies and tubulin-binding kinetics
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of enolase 1 in bone marrow-derived mast cells with calreticulin
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Merkulova, T.; Lucas, M.; Jabet, C.; Lamande, N.; Rouzeau, J.D.; Gros, F.; Lazar, M.; Keller, A.
Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins
Biochem. J.
323
791-800
1997
Mus musculus
Keller, A.; Peltzer, J.; Carpentier, G.; Horvath, I.; Olah, J.; Duchesnay, A.; Orosz, F.; Ovadi, J.
Interactions of enolase isoforms with tubulin and microtubules during myogenesis
Biochim. Biophys. Acta
1770
919-926
2007
Mus musculus (P17182), Mus musculus (P21550)
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