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Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00924
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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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neurosecretory
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pleomorphic
-
small-cell
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polygonal
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histogenesis
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epithelioid
-
dense-core
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polypoid
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myxoid
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out-of-hospital
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
(Z)-3-chloro-2-phosphoenolpyruvate + OH-
?
-
wild-type enzyme catalyzes hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3
-
-
?
D-tartronate semialdehyde phosphate
?
-
slowly-reacting strongly bound chromophoric substrate
-
-
?
D-tartronate semialdehyde-2-phosphate
?
-
substrate analogue that changes its spectrum while bound to the enzyme
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
in vitro studies on catalytic, divalent cation binding sites
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
influence on exchange of amino acid residues on structure, dissociation and function of enolase analyzed
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
separated role of enolase besides function in glycolysis, stimulation of vacuole fusion and involvement in protein trafficking to vacuoles determined
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
?
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
separated role of enolase besides function in glycolysis, stimulation of vacuole fusion and involvement in protein trafficking to vacuoles determined
-
-
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
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed
-
additional information
-
complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed
-
additional information
-
specific affinity to tRNA imported into mitochondria, involved to direct mitochondrial tRNA import in vitro
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
Co2+
-
activates in 0.1 M KCl, maximum activity at 0.0035 mM. Maximum of 4 Co2+ ions are bound per dimer
Mg2+
additional information
-
Ca2+, Ba2+, Sr2+, Hg2+, Pb2+, and Be2+ are not capable of activating the enzyme
Mg2+
two ions are necessary for activity, shows inhibition at high concentration
Mn2+
can replace Mg2+, mechanistic study using electron paramagnetic resonance
Zn2+
can replace Mg2+, mechanistic study using electron paramagnetic resonance
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphonoacetohydroxamate
preference for formation of hybrid Zn2+/Mn2+ complexes with enolase, in vitro activity of the complexed enolase in presence of phosphonoacetohydroxamate investigated by crystallography and electron paramagnetic resonance spectroscopy
Mg2+
-
inhibitor above 1 mM, N207A, H159A, H159N and H159F mutants are stimulated at this concentration
Mg2+
-
Mg2+ is inhibitory at 30 mM to the physiological reaction, but not to the reaction with D-tartronate semialdehyde phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
2-phospho-D-glycerate
-
Km ranges between 0.047 mM and 0.130 mM between pH 6.0 and pH 8.6
0.05
2-phospho-D-glycerate
K345A/N80D/N126D, 25°C, Mg2+, pH 7.5
0.032
2-phospho-D-glycerate
-
in presence of 1 mM Mg2+, native enzyme
0.03205
2-phospho-D-glycerate
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.04482
2-phospho-D-glycerate
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.05856
2-phospho-D-glycerate
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.131
2-phospho-D-glycerate
-
in presence of 1 mM Mg2+, mutant enzyme S39A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018 - 0.019
2-phospho-D-glycerate
-
mutant enzyme S39A, pH 7.8, 21-23°C
19.4
2-phospho-D-glycerate
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
19.7
2-phospho-D-glycerate
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
71.4
2-phospho-D-glycerate
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.327
Mg2+
-
isoform Err2p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
0.695
Mg2+
-
isoform Err3p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
2.1
Mg2+
-
isoform Eno1p, in 50 mM imidazole, pH 7.1, 250 mM KCl, 1 mM Mg(OAc)2, 0.1 mM EDTA, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
additional information
-
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl
additional information
enzyme activity monitored by following the conversion of phosphoenolpyruvate to 2-phospho-D-glycerate, specific activities of the variants, relative to wildtype enolase, are 0.1% for G157D and 0.01% for G376E
additional information
-
enzyme activity monitored by following the conversion of phosphoenolpyruvate to 2-phospho-D-glycerate, specific activities of the variants, relative to wildtype enolase, are 0.1% for G157D and 0.01% for G376E
additional information
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
-
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
-
additional and independent function beyond glycolytic enzyme function, involvement in mitochondrial tRNA targeting, depletion of enolase inhibits tRNA import in vivo, activity of enolase as an alternative molecular chaperone suggested
additional information
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
-
in vitro stimulation of vacuole fusion by recombinant enolase determined, no stimulation solely by addition of substrate or product of enolase, catalytic activity independent of role in vacuole fusion, enolase-deficient vacuoles lack in vitro stimulation, enolase deficiency prevents normal protein sorting to the vacuole
additional information
-
enolase shows the same specific activity (110 U/mg) in Tris-acetate or Tris-HCl buffers, whereas the specific activity is diminished (70 U/mg) in phosphate buffer
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
small portion of enolase bound to vacuoles, in vitro stimulation of vacuole fusion determined
small portion of enolase bound to vacuoles, in vitro stimulation of vacuole fusion determined
-
up to 7% of enolase activity associated with mitochondria, targeting towards the mitochondrial outer membrane, affinity to the mitochondrial surface more than 10fold higher for Eno2p than for Eno1p
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
far-UV CD spectroscopy after size-exclusion chromatography
46500
46672
-
x * 46672, isoform Eno1p, calculated from amino acid sequence
46673
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
47181
-
x * 47181, isoform Err3p, calculated from amino acid sequence
47184
-
x * 47184, isoform Err3p, electrospray ionization mass spectrometry
47196
-
x * 47196, isoform Err2p, calculated from amino acid sequence
47198
-
x * 47198, isoform Err2p, electrospray ionization mass spectrometry
96000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 46673, isoform Eno1p, electrospray ionization mass spectrometry
?
-
x * 47184, isoform Err3p, electrospray ionization mass spectrometry
?
-
x * 47198, isoform Err2p, electrospray ionization mass spectrometry
additional information
subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15°C for 24 h, spectrometrically measured
additional information
-
subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15°C for 24 h, spectrometrically measured
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
in vivo- and in vitro-glycation induce a considerable irreversible activity loss
additional information
-
in vivo- and in vitro-glycation induce a considerable irreversible activity loss
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
engineered K345A/N80D/N126D heterodimer in complex with substrate/product, 1.85A resolution, batch method
mutant E211Q complexed with Mg2+ and phosphoenolpyruvate, mutant E168Q complexed with Mg2+ and 2-phospho-D-glycerate
structure of enolase-Zn2+/Mn2+ complex formation with phosphonoacetohydroxamate solved to 1.54 A resolution by X-ray crystallography, replacement of native Mg2+ ions with Mn2+/Zn2+ introduces only minor atom displacements in the binding site, crystallographic data refined, simulations reveal a model of the enolase active site chosen for the study indicating sites MI and MII either occupied with Mn2+ at site MI and Zn2+ at site MII or vice versa, stereo view of the coordination of the two metal ions in the enolase-inhibitor-complex and of key active site residues presented, rotation patterns shown
co-crystallization of the S39A mutant with Mg2+ and phosphonoacetohydroxamate, the active-site flap is opened
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E168Q
the Mg2+ binding site is different compared to the wild type enzyme
E211Q
G157D
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
G376E
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
K345A/N80D/N126D
heterodimer with one inactive K345A subunit and one active N80D and N126D subunit
N80D/N126D
mutant with surface mutations to facilitate ion-exchange chromatographic separation
E168Q
E211Q
-
severely depressed activity, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate. Glu211 participates in the second step of the reaction
H159A
K345A
-
severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, fails to catalyze the exchange of the C-2 proton of 2-phospho-D-glycerate with deuterium in D2O, inactive in ionization of tartronate semialdehyde phosphate. Lys345 functions as the base in the ionization of 2-phosphoglycerate
S39A
additional information
E211Q
can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate
E168Q
-
the mutant has approximately 0.01% of the activity of native enolase. It binds 3-aminoenolpyruvate-2-phosphate, the 3-amino analogue of the product phosphoenolpyruvate and D-tartronate semialdehyde-2-phosphate, the aldehyde analogue of the substrate 2-phosphoglycerate, the latter two with affinities similar to those of the native enzyme
E168Q
-
severely depressed activity, does not catalyze hydrolysis of (Z)-3-chloro-2-phosphoenolpyruvate by addition of OH- and elimination of Cl- at C-3, alters the tautomeric state or catalyzes ionization of bound tartronate semialdehyde phosphate
H159A
-
mutation has no effect on conformation or enzyme-ligand complex, but yields an inactive enzyme
S39A
-
mutant of isoenzyme 1, relative maximal velocity of 0.01% and an activation constant for Mg2+ ca. 10fold higher, compared with the native enzyme
additional information
folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
-
folding studies, dissociation experiments, determination of thermal and enzymatic stability
additional information
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
-
impaired catalytic activity of enolase retains in vitro stimulation of fusion of isolated vacuoles, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
-
engineered enolase forms disrupted in catalytic activity retain features to direct mitochondrial import of tRNA
additional information
impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
additional information
-
impaired catalytic activity of enolase retains in vitro stimulation of vacuole fusion, partial inactivity of enolase diminishes vacuole fusion, enolase-deficient vacuoles lacks in vitro stimulation of vacuole fusion
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55.5
-
the melting temperature of isoform Eno1p, Err2, and Err3p are 55.5°C, 60.5°C, and 60°C, respectively
additional information
additional information
thermal stability lower in mutant forms of enolase, wild-type enolase has Tm of 55.4°C, whereas G367E and G157D reveals a Tm of 51.2°C and 49.9°C, respectively, addition of 50 microM phosphonoacetohydroxamate increases thermal stabilization of wildtype and G157D enolases, but not of G367E
additional information
-
thermal stability lower in mutant forms of enolase, wild-type enolase has Tm of 55.4°C, whereas G367E and G157D reveals a Tm of 51.2°C and 49.9°C, respectively, addition of 50 microM phosphonoacetohydroxamate increases thermal stabilization of wildtype and G157D enolases, but not of G367E
additional information
-
thermal stability is increased by divalent metal ions and binding to substrate, enzyme dissociates before denaturation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, for in vitro import assays into mitochondria and three-hybrid analysis
-
wild type and several mutant recombinant enzymes using chromatography on Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, His-tagging and GST-tagging of recombinant enolase protein
expression of the mutants E211Q and E168Q in Escherichia coli
inserted into pET-3a, expressed in Escherichia coli BL21-DE3, site-directed mutagenesis performed
expressed in Escherichia coli, His-tagging and GST-tagging of recombinant enolase protein
expression of the recombinant H159A and H159G mutants in Escherichia coli
-
over-expression in Escherichia coli strain BL21, expression vector pET3a, His-tagged recombinant protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
influence of enolase on membrane fusion of vacuoles and protein trafficking analyzed
molecular biology
molecular biology
influence of enolase on membrane fusion of vacuoles and protein trafficking analyzed
molecular biology
-
studies on mitochondrial import machinery of Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malmstroem, B.G.
Enolase
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
471-494
1961
Saccharomyces cerevisiae, Solanum tuberosum
-
Brewer, J.M.; Glover, C.V.C.; Holland, M.J.; Lebioda, L.
Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism
Biochim. Biophys. Acta
1383
351-355
1998
Saccharomyces cerevisiae
Entian, K.D.; Meurer, B.; Mecke, D.
Purification of three distinct enolase isoenzymes from yeast
Anal. Biochem.
132
225-228
1983
Saccharomyces cerevisiae
Rose, S.L.; Dickinson, L.C.; Westhead, E.W.
Kinetic and physical properties of Co2+ enolase
J. Biol. Chem.
259
4405-4413
1984
Saccharomyces cerevisiae
Brewer, J.M.; Robson, R.L.; Glover, C.V.C.; Holland, M.J.; Lebioda, L.
Preparation and characterization of the E168Q site-directed mutant of yeast enolase 1
Proteins Struct. Funct. Genet.
17
426-434
1993
Saccharomyces cerevisiae
Sangadala, V.S.; Glover, C.V.C.; Robson, R.L.; Holland, M.J.; Lebioda, L.; Brewer, J.M.
Preparation by site-directed mutagenesis and characterization of the E211Q mutant of yeast enolase 1
Biochim. Biophys. Acta
1251
23-31
1995
Saccharomyces cerevisiae
Poyner, R.R.; Laughlin, L.T.; Sowa, G.A.; Reed, G.H.
Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants
Biochemistry
35
1692-1699
1996
Saccharomyces cerevisiae
Zhang, E.; Brewer, J.M.; Minor, W.; Carreira, L.A.; Lebioda, L.
Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
Biochemistry
36
12526-12534
1997
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
Poyner, R.R.; Larsen, T.M.; Wong, S.W.; Reed, G.H.
Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase
Arch. Biochem. Biophys.
401
155-163
2002
Saccharomyces cerevisiae
Vinarov, D.A.; Nowak, T.
Role of His159 in yeast enolase catalysis
Biochemistry
38
12138-12149
1999
Saccharomyces cerevisiae
Poyner, R.R.; Cleland, W.W.; Reed, G.H.
Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme
Biochemistry
40
8009-8017
2001
Saccharomyces cerevisiae (P00924)
Sims, P.A.; Larsen, T.M.; Poyner, R.R.; Cleland, W.W.; Reed, G.H.
Reverse protonation is the key to general acid-base catalysis in enolase
Biochemistry
42
8298-8306
2003
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
Brewer, J.M.; Wampler, J.E.
A differential scanning calorimetric study of the effects of metal ions, substrate/product, substrate analogues and chaotropic anions on the thermal denaturation of yeast enolase 1
Int. J. Biol. Macromol.
28
213-218
2001
Saccharomyces cerevisiae
Brewer, J.M.; Glover, C.V.; Holland, M.J.; Lebioda, L.
Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H159F, and N207A enolases
J. Protein Chem.
22
353-361
2003
Saccharomyces cerevisiae
Sims, P.A.; Menefee, A.L.; Larsen, T.M.; Mansoorabadi, S.O.; Reed, G.H.
Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit
J. Mol. Biol.
355
422-431
2006
Saccharomyces cerevisiae (P00924)
Zhao, S.; Choy, B.S.; Kornblatt, M.J.
Effects of the G376E and G157D mutations on the stability of yeast enolase - a model for human muscle enolase deficiency
FEBS J.
275
97-106
2007
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
Entelis, N.; Brandina, I.; Kamenski, P.; Krasheninnikov, I.A.; Martin, R.P.; Tarassov, I.
A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae
Genes Dev.
20
1609-1620
2006
Saccharomyces cerevisiae
Carmieli, R.; Larsen, T.M.; Reed, G.H.; Zein, S.; Neese, F.; Goldfarb, D.
The catalytic Mn2+ sites in the enolase-inhibitor complex: crystallography, single-crystal EPR, and DFT calculations
J. Am. Chem. Soc.
129
4240-4252
2007
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
Decker, B.L.; Wickner, W.T.
Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast
J. Biol. Chem.
281
14523-14528
2006
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae (P00925), Saccharomyces cerevisiae
Hakobyan, D.; Nazaryan, K.
Investigation of interaction between enolase and phosphoglycerate mutase using molecular dynamics simulation
J. Biomol. Struct. Dyn.
23
625-633
2006
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
Gomes, R.A.; Oliveira, L.M.; Silva, M.; Ascenso, C.; Quintas, A.; Costa, G.; Coelho, A.V.; Sousa Silva, M.; Ferreira, A.E.; Ponces Freire, A.; Cordeiro, C.
Protein glycation in vivo: functional and structural effects on yeast enolase
Biochem. J.
416
317-326
2008
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
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
Sanchez-Miguel, D.S.; Romero-Jimenez, J.; Reyes-Lopez, C.A.; Cabrera-Avila, A.L.; Carrillo-Ibarra, N.; Benitez-Cardoza, C.G.
Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model
Protein J.
29
1-10
2010
Saccharomyces cerevisiae
Moreno-Vargas, L.M.; Carrillo-Ibarra, N.; Arzeta-Pino, L.; Benitez-Cardoza, C.G.
Thermal unfolding of apo- and holo-enolase from Saccharomyces cerevisiae: different mechanisms, similar activation enthalpies
Int. J. Biol. Macromol.
49
871-878
2011
Saccharomyces cerevisiae
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