BRENDA - Enzyme Database

Structure analysis of Entamoeba histolytica enolase

Schulz, E.C.; Tietzel, M.; Tovy, A.; Ankri, S.; Ficner, R.; Acta Crystallogr. Sect. D 67, 619-627 (2011)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
4.2.1.11
expression of GST-tagged ENO in Escherichia coli BL21 (DE3)
Entamoeba histolytica
Crystallization (Commentary)
EC Number
Crystallization
Organism
4.2.1.11
purified recombinant EhENO with two 2-phospho-D-glycerate substrate molecules bound at the two active sites, the protein solution contains 7.5 mg/ml protein in 100 mM Tris-HCl pH 7.5, 100 mM NaCl, 5 mM MgCl2, sitting-drop vapour-diffusion, 20C, mixing of equal volumes of precipitant solution, contraining 100 mM Bis-Tris, pH 5.5, 25% w/v PEG 3350, 200 mM ammonium sulfate, and protein solution, X-ray diffractrion structure determination and analysis at 1.9 A resolution, molecular replacement
Entamoeba histolytica
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Entamoeba histolytica
-
phosphoenolpyruvate + H2O
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.11
Entamoeba histolytica
C4LXE8
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.2.1.11
recombinant GST-tagged ENO from Escherichia coli BL21 (DE3) by glutathione affinity chromatography, cleavage of the GST tag, and gel filtration
Entamoeba histolytica
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
713621
Entamoeba histolytica
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
substrate binding in pre-catalytic state and during catalysis, recombinant enzyme, overview
713621
Entamoeba histolytica
phosphoenolpyruvate + H2O
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
4.2.1.11
dimer
in the crystal structure of 2-phospho-D-glycerate-complexed enzyme, ENO forms an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation, overview
Entamoeba histolytica
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.11
expression of GST-tagged ENO in Escherichia coli BL21 (DE3)
Entamoeba histolytica
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
4.2.1.11
purified recombinant EhENO with two 2-phospho-D-glycerate substrate molecules bound at the two active sites, the protein solution contains 7.5 mg/ml protein in 100 mM Tris-HCl pH 7.5, 100 mM NaCl, 5 mM MgCl2, sitting-drop vapour-diffusion, 20C, mixing of equal volumes of precipitant solution, contraining 100 mM Bis-Tris, pH 5.5, 25% w/v PEG 3350, 200 mM ammonium sulfate, and protein solution, X-ray diffractrion structure determination and analysis at 1.9 A resolution, molecular replacement
Entamoeba histolytica
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.11
2-phospho-D-glycerate
Entamoeba histolytica
-
phosphoenolpyruvate + H2O
-
-
r
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.11
recombinant GST-tagged ENO from Escherichia coli BL21 (DE3) by glutathione affinity chromatography, cleavage of the GST tag, and gel filtration
Entamoeba histolytica
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.11
2-phospho-D-glycerate
-
713621
Entamoeba histolytica
phosphoenolpyruvate + H2O
-
-
-
r
4.2.1.11
2-phospho-D-glycerate
substrate binding in pre-catalytic state and during catalysis, recombinant enzyme, overview
713621
Entamoeba histolytica
phosphoenolpyruvate + H2O
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.2.1.11
dimer
in the crystal structure of 2-phospho-D-glycerate-complexed enzyme, ENO forms an asymmetric dimer with one active site in the open conformation and the other active site in the closed conformation, overview
Entamoeba histolytica