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Literature summary for 1.2.3.6 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

Organism UniProt Comment Textmining
Entamoeba histolytica
-
-
-

Purification (Commentary)

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

Reaction

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
2.1
-
-
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

Cofactor Comment Organism Structure
FAD
-
Entamoeba histolytica