Abstract
Summary Rat liver fatty acid synthetase is inhibited by chloroacetyl CoA. The inhibition is rapid and results from the covalent transfer of chloroacetyl group to the enzyme. A stoichiometric relationship exists between the moles of inhibitor bound and the loss of enzyme activity for fatty acid synthesis. Two moles of inhibitor are bound for complete inactivation and this inhibition results from the loss of activity for the critical condensation-CO2 exchange component reaction. These and other data are consistent with the presence of two sites on the enzyme for condensation between enzyme bound acetyl-and malonyl groups.
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