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Enzymatic regulation of liver acetyl-CoA metabolism in relation to ketogenesis

Authors
Journal
Advances in Enzyme Regulation
0065-2571
Publisher
Elsevier
Publication Date
Volume
2
Identifiers
DOI: 10.1016/s0065-2571(64)80007-8
Keywords
  • Session Ii Gluconeogenesis In Various Physiological And Pathological Conditions
Disciplines
  • Biology

Abstract

Summary In the regulation of ketone body formation the citrate synthase reaction occupies a key position in determining the metabolic fate of liver acetyl-CoA. As a factor which might shift acetyl-CoA from the oxidative pathway into direction of acetoacetate condensation by blocking the citric acid cycle a decrease of liver oxalacetate has been found in diabetic and fat-fed ketotic rats. Furthermore, an inhibition of citrate synthase in vitro in the presence of physiological concentrations of palmityl-CoA was observed. The inhibition is competitive with respect to oxalacetate but not with respect to acetyl-CoA (“allosteric inhibition”) and can be partially reversed by serum albumin. The mode of action of palmityl-CoA which lowers the affinity of the enzyme for oxalacetate in association with the reduction in liver oxalacetate levels can be considered as a sensitive regulatory system for the control of ketone body formation in liver.

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