PYRUVIC ACID METABOLISM II

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Abstract
Suspensions of whole cells and vacuum-dried cells of S. faecalis, strain 10Cl, oxidize pyruvate to acetate and CO2, but cell-free extracts from these cells catalyze the breakdown of pyruvate predominantly to acetoin and CO2. Lower substrate concn. and the addition of glutathione shift the balance, with extracts, to favor pyruvate oxidation. Fractionation with ammonium sulfate and dialysis against citrate buffer yields a prepn. almost completely dependent upon cocarboxylase and manganous ions. In the presence of these cofactors, 2 moles of pyruvate are converted to one mole of acetoin and 2 moles of CO2. The extracts contain an active alpha-acetolactic acid decarboxylase. Acetaldehyde does not serve as an intermediate in acetoin formation. Neither phosphate nor "pyruvate oxidation factor" is required for acetoin formation. Indirect evidence has been obtained for the function of divalent ions in the alpha-acetolactic acid decarboxylase.

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