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Literature summary extracted from

  • Ernest, I.; Callens, M.; Uttaro, A.D.; Chevalier, N.; Opperdoes, F.R.; Muirhead, H.; Michels, P.A.
    Pyruvate kinase of Trypanosoma brucei: overexpression, purification, and functional characterization of wild-type and mutated enzyme (1998), Protein Expr. Purif., 13, 373-382.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.40 D-fructose diphosphate allosteric effector Trypanosoma brucei

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.40 F463V reduced affinity for fructose 1,6-diphosphate and fructose 2,6-diphosphate Trypanosoma brucei
2.7.1.40 R22G strongly reduced affinity for fructose 1,6-diphosphate and fructose 2,6-diphosphate Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.40 0.098 0.1 GDP pH 7.5, 25°C Trypanosoma brucei

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.40 Trypanosoma brucei
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.40 ADP + phosphoenolpyruvate
-
Trypanosoma brucei ATP + pyruvate
-
?
2.7.1.40 GDP + phosphoenolpyruvate
-
Trypanosoma brucei GTP + pyruvate
-
?

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.1.40 Trypanosoma brucei isoelectric focusing
-
7.95