Abstract
THE mitochondrial enzyme β-hydroxybutyrate dehydrogenase (BDH) catalyses the conversion of β-hydroxybutyrate to acetoacetate, with the subsequent production of three molecules of adenosine triphosphate for every molecule of β-hydroxybutyrate oxidized. Recent evidence suggests that this energy-yielding reaction is important for maintaining the metabolism of the brain when the supply of glucose is chronically depleted. Owen et al.1 demonstrated that β-hydroxybutyrate and acetoacetate become the principal sources of energy for the brain in humans subjected to prolonged starvation. The transition from glucose to ketones as the primary substrate for oxidative metabolism in the central nervous system occurs without demonstrable cerebral dysfunction1.
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