β-Hydroxybutyrate Dehydrogenase from Pseudomonas lemoignei

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).

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

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