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Literature summary extracted from

  • Michaels, G.; Milner, Y.; Reed, G.H.
    Magnetic resonance and kinetic studies of pyruvate, phosphate dikinase. Interaction of oxalate with the phosphorylated form of the enzyme (1975), Biochemistry, 14, 3213-3219.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.9.1 oxalate competitive to pyruvate, oxalate binds to the phosphorylated form of the enzyme [Clostridium] symbiosum

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.1 [Clostridium] symbiosum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate
-
[Clostridium] symbiosum AMP + phosphoenolpyruvate + diphosphate
-
?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.9.1 0.025
-
oxalate pH 7.5, 25ΒΊC [Clostridium] symbiosum