• 1 January 1984
    • journal article
    • research article
    • Vol. 7  (2) , 101-107
Abstract
Tumors of peripheral tissues contain low levels of succinyl coenzyme [CoA]-acetatoacetate CoA transferase activity which is not induced in vitro by prolonged cultivation in 2.5 mM DL-3-hydroxybutyrate. Although this enzyme is considered to be the main agent controlling the extent to which ketone bodies serve as metabolic substrates, such tumors metabolize D(-)-3-hydroxy[314C]butyrate to 14CO2. Also addition of 3-hydroxybutyrate and/or acetoacetate reduces the amount of 14CO2 produced from D-[uniformly labeled-14C] glucose suggesting a common metabolic intermediate. These observations can be accounted for by the presence of acetoacetyl-CoA synthetase, an enzyme which is able to synthesize acetoacetyl-CoA directly from actetoacetate, ATP and CoA. This is the 1st demonstration of this enzyme in tumor tissue. The rate of metabolism of acetoacetate by this enzyme is sufficient to account for the production of CO2 from 3-hydroxybutyrate.

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