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Literature summary extracted from

  • Kim, J.; Dunaway-Mariano, D.
    Phosphoenolpyruvate mutase catalysis of phosphoryl transfer in phosphoenolpyruvate: kinetics and mechanism of phosphorus-carbon bond formation (1996), Biochemistry, 35, 4628-4635.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.2.9 oxalate competitive Tetrahymena pyriformis
5.4.2.9 oxalylphosphate competitive Tetrahymena pyriformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.2.9 0.0035
-
Phosphonopyruvate 25°C, pH 7.5 Tetrahymena pyriformis
5.4.2.9 0.77
-
phosphoenolpyruvate 25°C, pH 7.5 Tetrahymena pyriformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.2.9 Mg2+ or Mn2+ required Tetrahymena pyriformis
5.4.2.9 Mn2+ or Mg2+ required Tetrahymena pyriformis

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.9 Tetrahymena pyriformis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.2.9 phosphoenolpyruvate
-
Tetrahymena pyriformis 3-phosphonopyruvate
-
r

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.4.2.9 0.032
-
oxalate 25°C, pH 7.5 Tetrahymena pyriformis
5.4.2.9 0.18
-
oxalylphosphate 25°C, pH 7.5 Tetrahymena pyriformis