Abstract
Abstract Citrate lyase from Aerobacter aerogenes undergoes inactivation during the course of the reaction which it catalyzes. Both the initial rate of reaction and the extent of reaction until complete inactivation are dependent on the nature of the metal ion and the amount of enzyme used. The inactivation has been attributed by others to an inhibition by enolic oxalacetate. We have also observed inhibition of the enzyme on preliminary incubation with oxalacetate, but high concentrations of either enol or keto forms are required to obtain significant inhibition. Constant removal of oxalacetate formed during the reaction by conversion to malate with the malate dehydrogenase system does not change either the rate of inactivation or the extent of reaction compared to the reaction in which oxalacetate is allowed to accumulate. Concentrations of oxalacetate, malate, NAD, NADH, and acetate that occur during the reaction, used either singly or in various combinations during a preliminary incubation, affect neither the initial rate nor the extent of the reaction.
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