Abstract
D-β-Hydroxybutyric dehy drogenase of respiratory particles from pig heart was first described in 1937 by Green, Dewan and Leloir 1 . With an assay based on oxygen uptake through the cytochrome system, they demonstrated that the enzyme was stereospecific for the D-isomer and that β-hydroxypropionic acid, αhydroxybutyric acid, γ-hydroxybutyric acid, crotonic acid, butyric acid, and acetic acid were not oxidized under conditions in which β-hydroxybutyrate was oxidized vigorously. The enzyme was shown to be distinct from malic and lactic dehydrogenases. The particulate enzyme also dehydrogenates higher d-β-hydroxy aliphatic acids up to nine carbon atoms long2, but does not act on l-β-hydroxyacids or their coenzyme A thioesters3. d-β-hydroxybutyric dehydrogenase is specific for DPN and will not reduce TPN1,3 or desamino-DPN4.
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