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Literature summary extracted from

  • Schulz, E.C.; Tietzel, M.; Tovy, A.; Ankri, S.; Ficner, R.
    Structure analysis of Entamoeba histolytica enolase (2011), Acta Crystallogr. Sect. D, 67, 619-627.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.11 expression of GST-tagged ENO in Escherichia coli BL21 (DE3) Entamoeba histolytica

Crystallization (Commentary)

EC Number Crystallization (Comment) 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, 20°C, 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.11 2-phospho-D-glycerate Entamoeba histolytica
-
 phosphoenolpyruvate + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.11 Entamoeba histolytica C4LXE8
-
-

Purification (Commentary)

EC Number Purification (Comment) 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.11 2-phospho-D-glycerate
-
 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 Entamoeba histolytica phosphoenolpyruvate + H2O
-
 r

Subunits

EC Number Subunits Comment 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

Synonyms

EC Number Synonyms Comment Organism
4.2.1.11 EhENO
-
 Entamoeba histolytica
4.2.1.11 enolase
-
 Entamoeba histolytica