3-hydroxybutyrate dehydrogenase

D- beta-hydroxybutyrate dehydrogenase ( BDH ) are called enzymes which catalyze the interconversion of acetoacetate to β - hydroxybutyrate and D- reverse. This equilibrium reaction is necessary for the structure of the Ketokörpers D - β - hydroxybutyrate in the liver of mammals, and its degradation in the tissues. From BDH two paralogous isoforms are known BDH1 is localized in the mitochondria and in the cytosol BDH2.

Also, in some bacteria BDH can be found. It enables, inter alia, special Acidovorax and Ralstonia pickettii strains that degrade the plastic polyhydroxybutyric. BDH can also be used for the rapid measurement of the ketone body content in the blood.

The amino acid sequence of BDH is identical to two-thirds of the short-chain alcohol dehydrogenases. Regarding the structures, they differ only in the substrate -binding domain and the phospholipid - binding site.

Catalysed equilibrium

NADH / H ⇔ NAD

Acetoacetate and hydroxybutyrate merge. Required for the allosteric activation of the enzymatic activity of BDH is phosphatidylcholine.

Human Genome Organisation Protein isoform Digital Object Identifier
211678
de