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The effect of divalent metal ions on the reaction catalyzed by pig heart citrate synthase has been investigated. Concentrations of divalent metal ions (Mn++, Mg++, and Ca++) in 100-fold excess of acetyl coenzyme A concentration inhibit the enzymic reaction. It is suggested that the inhibition is due to chelate formation between the divalent metal ions and the acetyl-CoA molecule, most likely at the polyphosphate chain of the molecule. The inhibition of pig heart citrate synthase by adenosine triphosphate and other nucleotides, palmitoyl-CoA, reduced nicotinamide adenine dinucleotide, and reduced nicotinamide adenine dinucleotide phosphate was studied. Divalent metal ions (Mn++, Mg++, and Ca++) at low concentrations reduce the inhibition. We suggest that the effect is due to the chelation of the metal ions with the polyphosphate moiety of the inhibitor molecules.
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Kosicki et al. (1966) studied this question.
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