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Literature summary for extracted from

  • Takeuchi, T.; Weinbach, E.C.; Diamond, L.S.
    Pyruvate oxidase (CoA acetylating) in Entamoeba histolytica (1975), Biochem. Biophys. Res. Commun., 65, 591-596.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information activity is not enhanced by phosphatidyl-choline, -inositol, and -ethanolamine or by artificial electron acceptors Entamoeba histolytica


Organism UniProt Comment Textmining
Entamoeba histolytica

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate, hydroxyapatite, partially purified Entamoeba histolytica


Reaction Comment Organism Reaction ID
pyruvate + CoA + O2 = acetyl-CoA + CO2 + H2O2 enzyme catalyzes transacetylation from pyruvate to CoA by an oxidase reaction in which H2O2 is produced Entamoeba histolytica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [Āµmol/min/mg] Specific Activity Maximum [Āµmol/min/mg] Comment Organism
Entamoeba histolytica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + O2
Entamoeba histolytica acetyl-CoA + CO2 + H2O2


Cofactor Comment Organism Structure
Entamoeba histolytica