Activation and Oxidation of Acetic Acid-1-C14 by Cell Free Homogenates of Germinating Peanut Cotyledons

Abstract
A soluble enzyme preparation having acetyl-thiokinase activity is described in homogenates of germinating peanut cotyledons. This enzyme is capable of activating acetic acid to acetyl coenzyme A in the presence of coenzyme A, adenosine triphosphate, and Mg ion. The oxidation of palmitic acid-11-C14 to C14O2 requires the presence of both a particulate fraction sedimenting like mitochondria, and a soluble protein fraction. Likewise synthetic acetyl coenzyme A requires both soluble and particulate components for oxidation of CO2. The extent of this oxidation is increased markedly by addition of glyoxylate.