Abstract
Two palmitoyl‐CoA synthetase activities have been demonstrated in rat liver microsomes. One, catalyzing palmitoyl‐CoA synthesis from ATP, palmitate and CoASH as well as from palmitoyl‐AMP and CoASH. A second enzyme reacts with the first constituents only and is inactive with palmitoyl‐AMP. The first enzyme, but not the second catalyzes the reaction between palmitoyl‐AMP and PPi to yield ATP and palmitic acid.This duality has been shown by: (a) partial separation of the two types of activity by fractional solution in Triton X‐100, (b) kinetic behaviour testing competition between both reaction mixtures at saturating concentrations and (c) the varying distribution of the two activities in microsomes obtained from rats under different dietary regimes or when diabetes was induced by alloxan.
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