Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Homo sapiens

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Homo sapiens


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
4.2.1.11
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RECOMMENDED NAME
GeneOntology No.
phosphopyruvate hydratase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
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elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1-butanol autotrophic biosynthesis (engineered)
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Bifidobacterium shunt
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Entner-Doudoroff pathway I
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Entner-Doudoroff pathway II (non-phosphorylative)
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Entner-Doudoroff pathway III (semi-phosphorylative)
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ethylene biosynthesis V (engineered)
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formaldehyde assimilation I (serine pathway)
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gluconeogenesis I
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gluconeogenesis II (Methanobacterium thermoautotrophicum)
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gluconeogenesis III
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glycerol degradation to butanol
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glycolysis I (from glucose 6-phosphate)
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glycolysis II (from fructose 6-phosphate)
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glycolysis III (from glucose)
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glycolysis IV (plant cytosol)
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glycolysis V (Pyrococcus)
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heterolactic fermentation
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photosynthetic 3-hydroxybutanoate biosynthesis (engineered)
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Rubisco shunt
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superpathway of glucose and xylose degradation
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glycolysis
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Glycolysis / Gluconeogenesis
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Methane metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
show the reaction diagram
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-
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?
2-phospho-D-glycerate
?
show the reaction diagram
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the enzyme is a plasminogen binding protein
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2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
D-tartronate semialdehyde phosphate
?
show the reaction diagram
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slowly-reacting strongly bound chromophoric substrate
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-
?
additional information
?
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
show the reaction diagram
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-
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-
?
2-phospho-D-glycerate
?
show the reaction diagram
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the enzyme is a plasminogen binding protein
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2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
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r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
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r
additional information
?
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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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxy-2-nonenal
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acrolein
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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
Mn2+
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inhibitory in excess
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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phosphate
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at a high phosphate concentration, noncompetitive inhibition is found and at a lower concentration competitive inhibition
PO43-
mimics the phosphate group of substrate
trans-2-nonenal
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Zn2+
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inhibitory in excess
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.199 - 0.66
2-phospho-D-glycerate
0.22 - 0.3
2-phosphoglycerate
0.58 - 0.83
phosphoenolpyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
81.68
2-phospho-D-glycerate
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
34.07
phosphoenolpyruvate
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
410
2-phospho-D-glycerate
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
48.5
phosphoenolpyruvate
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.8
fluoride
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at low phosphate concentrations (4-6 mM), in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
14.37
Mg2+
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
3.04
Mn2+
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.32
phosphate
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
1.58
Zn2+
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in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.9
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crude extract, at pH 6.8
69.6
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75
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after 83fold purification, at pH 6.8
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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phosphate buffer
7.4 - 7.6
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R-NSE, Y-NSE, Y-NSE.H6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA complexes with annexin A2, cytokeratin 8 and tissue-type plasminogen activator in raft membrane fractions of pancreatic cancer cells
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
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testicular, epididymal and ejaculated
Manually annotated by BRENDA team
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ENOA is upregulated
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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2 * 45000, SDS-PAGE
46000
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x * 46000, enzyme R-NSE, enzyme Y-NSE, SDS-PAGE
51000
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His-tagged enzyme, SDS-PAGE
62000
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gel filtration
93000
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gel filtration
100000
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sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 45000, SDS-PAGE
monomer
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1 * 50000, gel filtration
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
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alkylation
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methylation
phosphoprotein
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side-chain modification
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acetylation, methylation
additional information
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ENOA in tumor cells is subjected to more acetylation, methylation and phoshorylation than in normal tissues
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.7 A resolution by multiwavelength anomalous diffraction and molecular replacement techniques
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asymmetric complex NSE*Mg2SO4/NSE*MgCl, pH 7.0, large orthorhombic plates, structure by molecular replacement
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at room temperature using the hanging-drop vapour-diffusion method for structure analysis by X-ray diffraction
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enolase fluoride/phosphate inhibitory complex and enolase phosphate inhibitory complex
hanging drop vapor diffusion method, using 0.1 M ammonium acetate, 0.1 M bis-tris pH 5.5, 20% (w/v) polyethylene glycol monomethyl ether 2000
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme maintains only 5% of the initial catalytic activity upon glycation for the first 90 min
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-enolase and gamma,gamma-enolase
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ammonium sulfate precipitation, DEAE-Sephadex A-50 gel filtration, CM-Sephadex gel filtration, and QAE-Sephadex gel filtration
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DEAE and carboxymethyl columns, oligonucleotide affinity column
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glutathione-Sepharose 4B bead chromatography, gel filtration
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HiTrap Ni2+-chelating column chromatography and Superdex 75 gel filtration
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isoforms S1, S2, S3
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native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
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Ni-NTA Sepharose, ion-exchange chromatography, ammonium sulfate precipitation
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Ni2+-affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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expression in Escherichia coli strain JM109 with C-terminal His-tag
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expression in Escherichia coli; 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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subcloned in Escherichia coli
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-enolase is consistently up-regulated from mild cognitive impairment to Alzheimer's disease
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alpha-enolase is overexpressed at both mRNA and protein levels in pancreatic ductal adenocarcinoma cells
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alpha-enolase is up-regulated in pancreatic ductal adenocarcinoma
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ENOA expression is enhanced in diverse cancer cell types, e.g. cell surface ENOA in breast cancer cells, overview
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In human follicular thyroid carcinoma cells, retinoic acid causes a decrease in ENOA levels that coincides with their reduced motility
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lipopolysaccharide rapidly up-regulates ENO-1 cell-surface expression
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine