β-Hydroxybutyrate Dehydrogenase from Pseudomonas lemoignei

D-β-hydroxybutyrate dehydrogenase (BDH) is a membrane bound lipid-requiring enzyme.

β-Hydroxybutyrate Dehydrogenase from Pseudomonas lemoignei has been used in coupled assay to confirm the formation of acetoacetate.

Suitable for the determination of acetoacetate and D(-)-3-hydroxybutyrate by the method of Williamson, D. H., and Mellanby, J., Methods of Enzymatic Analysis, Bergmeyer, H., ed., 2nd edition, 4, 1836 (1974).

In Paracoccus denitrificans, 3-hydroxybutyrate dehydrogenase plays a key role in the degradation of intracellular polyhydroxybutyrate and polyhydroxyvalerate.

In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle).

One unit will oxidize 1.0 μmole of D-β-hydroxybutyrate to acetoacetate per min at pH 7.8 at 37 °C.

lyophilized powder containing sucrose, β-NAD and Tris buffer salts