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Literature summary for 2.7.9.1 extracted from

  • Carroll, L.J.; Xu, Y.; Thrall, S.H.; Martin, B.M.; Dunaway-Mariano, D.
    Substrate binding domains in pyruvate phosphate dikinase (1994), Biochemistry, 33, 1134-1142.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
[Clostridium] symbiosum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate contains several structural domains. The catalytic histidine, the pyruvate binding site and the ATP binding site are located in different domains >#4# two-step bi bi uni uni mechanism <20> [Clostridium] symbiosum

Substrates and Products (Substrate)

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