Abstract
The inhibitory action of fluoromalate, fluoroacetoacetates and fluorocitrate was studied in pigeon liver particulate, rat liver mitochondrial and isolated enzyme systems. The results show that fluoromalate and fluorocitrate increase acetoacetate formation from pyruvate and CO 2 with concomitant depression of citrate synthesis in rat liver mitochondria but with an accumulation of citrate by the pigeon particles in presence of fluorocitrate. Fluoroacetoacetates are inhibitory to both acetoacetate and citrate synthesis, particularly in rat liver mitochondria. Kidney cortex but not liver homogenates rapidly hydrolyze the fluoroacetoacetates to fluoroacetate. Considerable inhibition of the malic enzyme by fluoromalate and 2,4-fluoroacetoacetate was observed, while none of the inhibitors affected oxalacetate decarboxylase. Only fluoromalate inhibited oxalacetate carboxylase and DPN-dependent malic dehydrogenase. Fluoromalate, fluorocitrate and fluoroacetoacetates inhibited β-hydroxybutyrate oxidation, but only the fluoroacetoacetates inhibited significantly the acetoacetate-synthesizing enzyme. Acetothiokinase, fumarase, and isocitric (TPN) and succinic dehydrogenases were not inhibited by any of the fluoro compounds. Several aspects of the kinetics of inhibition have been examined.
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