Differential inhibition of ketogenesis by malonyl-CoA in mitochondria from fed and starved rats

Abstract

Rates of ketogenesis in mitochondria from fed or starved rats were identical at optimal substrate concentrations, but responded differently to inhibition by malonyl-CoA. The Ki for malonyl-CoA is apparently greater in the starved animal. For the regulation of ketogenesis in the starved state, the lower sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA may be more important than the concentration of malonyl-CoA.