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1.1
-
H159N mutant, pH 7.8, 21ºC
1.9
-
H159F mutant, pH 7.8, 21ºC
248
-
N207A mutant, pH 7.8, 21ºC
3.3
-
H159A mutant, pH 7.8, 21ºC
442
-
wild type, pH 7.8, 21ºC
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
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
-
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
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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
H159F
-
less than 1% of the activity compared to the wild type
H159N
-
less than 1% of the activity compared to the wild type
K345A/N80D/N126D
heterodimer with one inactive K345A subunit and one active N80D and N126D subunit
N207A
-
50% of the activity compared to the wild type
N80D/N126D
mutant with surface mutations to facilitate ion-exchange chromatographic separation
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
E168Q
the Mg2+ binding site is different compared to the wild type enzyme
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
E211Q
can exchange the alpha proton of 2-phospho-D-glycerate, but cannot catalyze the complete dehydration to phosphoenolpyruvate
E211Q
inactive, but properly folded
H159A
-
less than 1% of the activity compared to the wild type
H159A
-
mutation has no effect on conformation or enzyme-ligand complex, but yields an inactive enzyme
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
-
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
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
additional information
-
engineered enolase forms disrupted in catalytic activity retain features to direct mitochondrial import of tRNA
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
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Malmstroem, B.G.
Enolase
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
471-494
1961
Saccharomyces cerevisiae, Solanum tuberosum
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Purification of three distinct enolase isoenzymes from yeast
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Rose, S.L.; Dickinson, L.C.; Westhead, E.W.
Kinetic and physical properties of Co2+ enolase
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1984
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Preparation and characterization of the E168Q site-directed mutant of yeast enolase 1
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17
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1993
Saccharomyces cerevisiae
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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
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1995
Saccharomyces cerevisiae
brenda
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
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1996
Saccharomyces cerevisiae
brenda
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
brenda
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
brenda
Vinarov, D.A.; Nowak, T.
Role of His159 in yeast enolase catalysis
Biochemistry
38
12138-12149
1999
Saccharomyces cerevisiae
brenda
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)
brenda
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
brenda
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
brenda
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
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22
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2003
Saccharomyces cerevisiae
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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
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355
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2006
Saccharomyces cerevisiae (P00924)
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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
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2007
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
brenda
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
brenda
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
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Decker, B.L.; Wickner, W.T.
Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast
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281
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2006
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae (P00925), Saccharomyces cerevisiae
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Hakobyan, D.; Nazaryan, K.
Investigation of interaction between enolase and phosphoglycerate mutase using molecular dynamics simulation
J. Biomol. Struct. Dyn.
23
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2006
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
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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
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2008
Saccharomyces cerevisiae (P00924), Saccharomyces cerevisiae
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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
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584
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2010
Saccharomyces cerevisiae, Homo sapiens
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Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model
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29
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2010
Saccharomyces cerevisiae
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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
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2011
Saccharomyces cerevisiae
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The Saccharomyces cerevisiae enolase-related regions encode proteins that are active enolases
Yeast
30
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2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4743
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