Summary: D(—)-β-hydroxybutyrate dehydrogenase (BOHB-DH) (EC was purified 991-fold from Cd. Its specific activity was 5650 units (mg protein) min. The enzyme is a tetramer, with identical subunits and a total molecular mass of 100 kDa. BOHB-DH is not a glycoprotein. It is acidic and contains six disulphide bonds without free -SH groups. Under the assay conditions used, BOHB-DH activity was maximal at pH 8.0 and at 36 °C. The enzyme is an NAD oxidoreductase, and is inhibited by NADPH and NADH. It has high affinity for β-hydroxybutyrate: the value for the β-hydroxybutyrate substrate is 1 mM. Adenosine phosphates, pyruvate, acetyl-coenzyme A, oxaloacetate and 2-oxoglutarate inhibited purified BOHB-DH.


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