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

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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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14-3-2 protein
-
-
2-phospho-D-glycerate hydro-lyase
-
-
-
-
2-phospho-D-glycerate hydrolyase
2-phosphoglycerate dehydratase
-
-
-
-
2-phosphoglycerate enolase
-
-
-
-
2-phosphoglyceric dehydratase
-
-
-
-
2-phosphopyruvate hydrolyase
-
-
alpha,alpha-enolase
-
-
-
-
alpha-enolase
Alt a XI
-
-
-
-
beta,beta-enolase
-
-
-
-
beta-enolase
-
-
Cla h VI
-
-
-
-
Eno-alpha
-
-
ENO-S
-
-
Eno2
-
-
ENOA
-
-
enolase
enolase 2
-
-
enolase alpha
-
-
enolase gamma
-
-
enolase S
-
-
enolase-1
-
-
enolase-alpha
-
-
Enolase-phosphatase E1
-
-
gamma,gamma-enolase
-
-
-
-
gamma-enolase
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
-
-
-
-
OSE1
-
-
-
-
phosphoenolpyruvate hydratase
-
-
-
-
Phosphopyruvate hydratase
-
-
-
-
R-NSE
-
-
-
-
Skeletal muscle enolase
-
-
-
-
Tau-crystallin
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
-
-
elimination
-
-
-
-
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
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
?
show the reaction diagram
-
the enzyme is a plasminogen binding protein
-
-
?
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
-
slowly-reacting strongly bound chromophoric substrate
-
-
?
additional information
?
-
-
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
-
-
?
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
2,3-dioxo-5-methylthio-1-phosphopentane + 4 H+
3-hydroxy-5-methyl-thio-pent-2-en-1-yl-phosphate + H2O
show the reaction diagram
-
-
-
-
?
2-phospho-D-glycerate
?
show the reaction diagram
-
the enzyme is a plasminogen binding protein
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxy-2-nonenal
-
-
acrolein
-
-
fluoride
-
the inhibitory effect of fluoride alone is noncompetitive, but it is competitive in the presence of a low phosphate level
methylglyoxal
Mn2+
-
inhibitory in excess
p19ras
-
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
-
phosphate
-
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
-
-
Zn2+
-
inhibitory in excess
additional information
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.199 - 0.66
2-phospho-D-glycerate
0.58 - 0.83
phosphoenolpyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
81.68
2-phospho-D-glycerate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
34.07
phosphoenolpyruvate
-
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
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
48.5
phosphoenolpyruvate
-
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
-
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+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
3.04
Mn2+
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
0.32
phosphate
-
in 50 mM imidazole-HCl buffer, pH 6.8, with 3 mM MgSO4, 0.4 M KCl
1.58
Zn2+
-
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
-
crude extract, at pH 6.8
69.6
-
-
75
-
after 83fold purification, at pH 6.8
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
phosphate buffer
7.4 - 7.6
-
R-NSE, Y-NSE, Y-NSE.H6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
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
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
-
testicular, epididymal and ejaculated
Manually annotated by BRENDA team
-
ENOA is upregulated
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENOA_HUMAN
434
0
47169
Swiss-Prot
other Location (Reliability: 2)
ENOB_HUMAN
434
0
46987
Swiss-Prot
other Location (Reliability: 2)
ENO4_HUMAN
625
0
68465
Swiss-Prot
other Location (Reliability: 1)
ENOG_HUMAN
434
0
47269
Swiss-Prot
other Location (Reliability: 1)
A4QMW8_HUMAN
135
0
14536
TrEMBL
other Location (Reliability: 2)
A8K3B0_HUMAN
434
0
47313
TrEMBL
other Location (Reliability: 1)
A0A024R4F1_HUMAN
434
0
47169
TrEMBL
other Location (Reliability: 2)
K7EKN2_HUMAN
212
0
22514
TrEMBL
other Location (Reliability: 2)
K7EM90_HUMAN
195
0
21020
TrEMBL
other Location (Reliability: 2)
Q9NPL4_HUMAN
154
0
16939
TrEMBL
other Location (Reliability: 2)
A0A2R8YEM5_HUMAN
171
0
18381
TrEMBL
other Location (Reliability: 2)
U3KQP4_HUMAN
73
0
8122
TrEMBL
other Location (Reliability: 1)
F5H0C8_HUMAN
315
0
34762
TrEMBL
other Location (Reliability: 1)
D3DTL4_HUMAN
341
0
36848
TrEMBL
other Location (Reliability: 2)
B4DUJ6_HUMAN
273
0
29527
TrEMBL
other Location (Reliability: 2)
E5RGZ4_HUMAN
283
0
30403
TrEMBL
other Location (Reliability: 2)
A0A2R8Y6G6_HUMAN
434
0
47327
TrEMBL
other Location (Reliability: 2)
A0A5H1ZRQ0_HUMAN
422
0
45848
TrEMBL
other Location (Reliability: 2)
U3KQQ1_HUMAN
86
0
9482
TrEMBL
other Location (Reliability: 1)
A4UCS8_HUMAN
166
0
17788
TrEMBL
other Location (Reliability: 1)
A0A5H1ZRS3_HUMAN
628
0
68761
TrEMBL
other Location (Reliability: 1)
L0R849_HUMAN
388
0
42342
TrEMBL
other Location (Reliability: 2)
E2DRY6_HUMAN
338
0
36555
TrEMBL
other Location (Reliability: 2)
Q6FHV6_HUMAN
434
0
47269
TrEMBL
other Location (Reliability: 1)
K7EPM1_HUMAN
196
0
20922
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
sucrose density gradient centrifugation
45000
-
2 * 45000, SDS-PAGE
46000
-
x * 46000, enzyme R-NSE, enzyme Y-NSE, SDS-PAGE
47000
48000
50000
51000
His-tagged enzyme, SDS-PAGE
62000
-
gel filtration
93000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
2 * 45000, SDS-PAGE
monomer
1 * 50000, gel filtration
additional information
-
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
-
-
alkylation
-
methylation
phosphoprotein
-
-
side-chain modification
-
acetylation, methylation
additional information
-
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
-
asymmetric complex NSE*Mg2SO4/NSE*MgCl, pH 7.0, large orthorhombic plates, structure by molecular replacement
-
at room temperature using the hanging-drop vapour-diffusion method for structure analysis by X-ray diffraction
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme maintains only 5% of the initial catalytic activity upon glycation for the first 90 min
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-enolase and gamma,gamma-enolase
-
ammonium sulfate precipitation, DEAE-Sephadex A-50 gel filtration, CM-Sephadex gel filtration, and QAE-Sephadex gel filtration
-
DEAE and carboxymethyl columns, oligonucleotide affinity column
-
glutathione-Sepharose 4B bead chromatography, gel filtration
-
HiTrap Ni2+-chelating column chromatography and Superdex 75 gel filtration
isoforms S1, S2, S3
-
native enzyme from muscle by ammonium sulfate fractionation and ion exchange chromatography
-
Ni-NTA Sepharose, ion-exchange chromatography, ammonium sulfate precipitation
-
Ni2+-affinity column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli strain JM109 with C-terminal His-tag
-
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
-
subcloned in Escherichia coli
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-enolase is consistently up-regulated from mild cognitive impairment to Alzheimer's disease
-
alpha-enolase is overexpressed at both mRNA and protein levels in pancreatic ductal adenocarcinoma cells
-
alpha-enolase is up-regulated in pancreatic ductal adenocarcinoma
-
ENOA expression is enhanced in diverse cancer cell types, e.g. cell surface ENOA in breast cancer cells, overview
-
In human follicular thyroid carcinoma cells, retinoic acid causes a decrease in ENOA levels that coincides with their reduced motility
-
lipopolysaccharide rapidly up-regulates ENO-1 cell-surface expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baranowski, T.; Wolna, E.
Enolase from human muscle
Methods Enzymol.
42C
335-338
1975
Homo sapiens
Manually annotated by BRENDA team
Hullin, D.A.; Brown, K.; Kynoch, P.A.M.; Smith, C.; Thompson, R.J.
Purification, radioimmunoassay, and distribution of human brain 14-3-2 protein (nervous-system specific enolase) in human tissues
Biochim. Biophys. Acta
628
98-108
1980
Homo sapiens
Manually annotated by BRENDA team
Shimizu, A.; Suzuki, F.; Kato, K.
Purification of two enolases from human brain using a chromatofocusing column
Biochim. Biophys. Acta
717
348-354
1982
Homo sapiens
Manually annotated by BRENDA team
McAleese, S.M.; Thomson, F.E.; Dunbar, B.; Fothergill, J.E.
Human alpha-enolase and gamma-enolase: purification and amino acid sequence comparisons
Biochem. Soc. Trans.
15
377-378
1987
Homo sapiens
-
Manually annotated by BRENDA team
Andronicos, N.M.; Ranson, M.; Bognacki, J.; Baker, M.S.
The human ENO1 gene product (recombinant human alpha-enolase) displays characteristics required for a plasminogen binding protein
Biochim. Biophys. Acta
1337
27-39
1997
Homo sapiens
Manually annotated by BRENDA team
Kaneta, M.; Aoki, T.; Onagi, H.; Morikawa, J.; Watabe, H.
Biochemical and immunochemical properties of modified human neuron-specific enolase
Biol. Pharm. Bull.
20
556-559
1997
Homo sapiens
Manually annotated by BRENDA team
Qin, J.; Chai, G.; Brewer, J.M.; Lovelace, L.L.; Lebioda, L.
Fluoride Inhibition of Enolase: Crystal Structure and Thermodynamics
Biochemistry
45
793-800
2006
Homo sapiens (P09104), Homo sapiens
Manually annotated by BRENDA team
Force, A.; Viallard, J.L.; Saez, F.; Grizard, G.; Boucher, D.
Electrophoretic characterization of the human sperm-specific enolase at different stages of maturation
J. Androl.
25
824-829
2004
Homo sapiens
Manually annotated by BRENDA team
Wang, W.; Wang, L.; Endoh, A.; Hummelke, G.; Hawks, C.L.; Hornsby, P.J.
Identification of alpha-enolase as a nuclear DNA-binding protein in the zona fasciculata but not the zona reticularis of the human adrenal cortex
J. Endocrinol.
184
85-94
2005
Homo sapiens
Manually annotated by BRENDA team
Chai, G.; Brewer, J.M.; Lovelace, L.L.; Aoki, T.; Minor, W.; Lebioda, L.
Expression, purification and the 1.8 angstroms resolution crystal structure of human neuron specific enolase
J. Mol. Biol.
341
1015-1021
2004
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Pang, H.; Bartlam, M.; Rao, Z.
Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase Activity
J. Mol. Biol.
348
917-926
2005
Homo sapiens
Manually annotated by BRENDA team
Kang, H.J.; Jung, S.K.; Kim, S.J.; Chung, S.J.
Structure of human alpha -enolase (hENO1), a multifunctional glycolytic enzyme
Acta Crystallogr. Sect. D
D64
651-657
2008
Homo sapiens (P06733), Homo sapiens
Manually annotated by BRENDA team
Hsu, K.W.; Hsieh, R.H.; Lee, Y.H.; Chao, C.H.; Wu, K.J.; Tseng, M.J.; Yeh, T.S.
The activated Notch1 receptor cooperates with alpha-enolase and MBP-1 in modulating c-myc activity
Mol. Cell. Biol.
28
4829-4842
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Zhou, Y.F.; Li, L.F.; Su, X.D.
Crystallization and preliminary X-ray analysis of human liver alpha-enolase
Acta Crystallogr. Sect. F
65
288-290
2009
Homo sapiens (P06733), Homo sapiens
Manually annotated by BRENDA team
Pietkiewicz, J.; Bednarz-Misa, I.; Jermakow, K.; Gamian, A.
Enolase from Klebsiella pneumoniae and human muscle cells II. Kinetic parameters and sensitivity to fluoride and phosphate inhibitors
Adv. Clin. Exp. Med.
18
221-233
2009
Homo sapiens, Klebsiella pneumoniae
-
Manually annotated by BRENDA team
Bednarz-Misa, I.; Pietkiewicz, J.; Bana?, T.; Gamian, A.
Enolase from Klebsiella pneumoniae and human muscle cells. I. Purification and comparative molecular studies
Adv. Clin. Exp. Med.
18
71-78
2009
Homo sapiens, Klebsiella pneumoniae
-
Manually annotated by BRENDA team
Wygrecka, M.; Marsh, L.M.; Morty, R.E.; Henneke, I.; Guenther, A.; Lohmeyer, J.; Markart, P.; Preissner, K.T.
Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung
Blood
113
5588-5598
2009
Homo sapiens
Manually annotated by BRENDA team
Tu, S.H.; Chang, C.C.; Chen, C.S.; Tam, K.W.; Wang, Y.J.; Lee, C.H.; Lin, H.W.; Cheng, T.C.; Huang, C.S.; Chu, J.S.; Shih, N.Y.; Chen, L.C.; Leu, S.J.; Ho, Y.S.; Wu, C.H.
Increased expression of enolase alpha in human breast cancer confers tamoxifen resistance in human breast cancer cells
Breast Cancer Res. Treat.
121
539-553
2010
Homo sapiens
Manually annotated by BRENDA team
Jang, S.M.; Kim, J.W.; Kim, C.H.; Kim, D.; Rhee, S.; Choi, K.H.
p19(ras) Represses proliferation of non-small cell lung cancer possibly through interaction with neuron-specific enolase (NSE)
Cancer Lett.
289
91-98
2010
Homo sapiens
Manually annotated by BRENDA team
Al-Rawi, N.H.; Atiyah, K.M.
Salivary neuron specific enolase: an indicator for neuronal damage in patients with ischemic stroke and stroke-prone patients
Clin. Chem. Lab. Med.
47
1519-1524
2009
Homo sapiens
Manually annotated by BRENDA team
Brewer, J.M.; McKinnon, J.S.; Phillips, R.S.
Stopped-flow studies of the reaction of D-tartronate semialdehyde-2-phosphate with human neuronal enolase and yeast enolase 1
FEBS Lett.
584
979-983
2010
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Cappello, P.; Tomaino, B.; Chiarle, R.; Ceruti, P.; Novarino, A.; Castagnoli, C.; Migliorini, P.; Perconti, G.; Giallongo, A.; Milella, M.; Monsurro, V.; Barbi, S.; Scarpa, A.; Nistico, P.; Giovarelli, M.; Novelli, F.
An integrated humoral and cellular response is elicited in pancreatic cancer by alpha-enolase, a novel pancreatic ductal adenocarcinoma-associated antigen
Int. J. Cancer
125
639-648
2009
Homo sapiens
Manually annotated by BRENDA team
Pietkiewicz, J.; Gamian, A.; Staniszewska, M.; Danielewicz, R.
Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products
J. Enzyme Inhib. Med. Chem.
24
356-364
2009
Homo sapiens
Manually annotated by BRENDA team
Butterfield, D.A.; Lange, M.L.
Multifunctional roles of enolase in Alzheimers disease brain: beyond altered glucose metabolism
J. Neurochem.
111
915-933
2009
Homo sapiens
Manually annotated by BRENDA team
Zhou, W.; Capello, M.; Fredolini, C.; Piemonti, L.; Liotta, L.A.; Novelli, F.; Petricoin, E.F.
Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells
J. Proteome Res.
9
2929-2936
2010
Homo sapiens
Manually annotated by BRENDA team
Hakobyan, D.; Nazaryan, K.
Molecular dynamics study of interaction and substrate channeling between neuron-specific enolase and B-type phosphoglycerate mutase
Proteins Struct. Funct. Bioinform.
78
1691-1704
2010
Homo sapiens
Manually annotated by BRENDA team
Seweryn, E.; Pietkiewicz, J.; Bednarz-Misa, I.S.; Ceremuga, I.; Saczko, J.; Kulbacka, J.; Gamian, A.
Localization of enolase in the subfractions of a breast cancer cell line
Z. Naturforsch. C
64
754-758
2009
Homo sapiens
Manually annotated by BRENDA team
Capello, M.; Ferri-Borgogno, S.; Cappello, P.; Novelli, F.
alpha-Enolase: a promising therapeutic and diagnostic tumor target
FEBS J.
278
1064-1074
2011
Homo sapiens
Manually annotated by BRENDA team
Pietkiewicz, J.; Bronowicka-Szyde?ko, A.; Dzierzba, K.; Danielewicz, R.; Gamian, A.
Glycation of the muscle-specific enolase by reactive carbonyls: effect of temperature and the protection role of carnosine, pyridoxamine and phosphatidylserine
Protein J.
30
149-158
2011
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team