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Literature summary extracted from

  • Landa, A.; Rojo-Dominguez, A.; Jimenez, L.; Fernandez-Velasco, D.A.
    Sequencing, expression and properties of triosephosphate isomerase from Entamoeba histolytica (1997), Eur. J. Biochem., 247, 348-355.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.1 expression as wild-type enzyme and fusion protein with an N-terminal tail of six histidine residues Entamoeba histolytica

General Stability

EC Number General Stability Organism
5.3.1.1 at a concentration of 2 ng/ml or 0.4 ng/ml stable for 24 h Entamoeba histolytica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.1 53300
-
gel filtration Trypanosoma brucei

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.1 Entamoeba histolytica
-
-
-
5.3.1.1 Trypanosoma brucei
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.1
-
Entamoeba histolytica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.1 D-Glyceraldehyde 3-phosphate
-
Entamoeba histolytica Glycerone phosphate
-
?
5.3.1.1 D-Glyceraldehyde 3-phosphate
-
Trypanosoma brucei Glycerone phosphate
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.3.1.1 50
-
10 min, complete loss of activity Trypanosoma brucei
5.3.1.1 50
-
50 min, no loss of activity Entamoeba histolytica