3-hydroxybutyrate dehydrogenase 2 (HBDH2)

3-hydroxybutyrate dehydrogenase is a mitochondrial enzyme (commonly known as BDH1 in humans) that catalyzes the reversible conversion of (R)-3-hydroxybutyrate to acetoacetate, using NAD^+ as a cofactor and generating NADH in the process. It plays a key role in ketone body metabolism, mediating the interconversion of ketone bodies during fasting, starvation, diabetes, and other metabolic conditions. The enzyme is part of the short-chain dehydrogenase/reductase (SDR) superfamily and is found in mitochondria, with possible cytosolic versions in some organisms (sometimes referred to as BDH2). The precise definition and functions of "3-hydroxybutyrate dehydrogenase 2" (BDH2) versus the canonical mitochondrial form (BDH1) remain an area of ongoing research and some nomenclature confusion. *If you require the standardized gene/protein in human clinical pharmacology, refer to "3-hydroxybutyrate dehydrogenase, mitochondrial" (BDH1); for the cytosolic mammalian paralog, search for BDH2 and confirm relevant functional data before application.*

Other names

3-hydroxybutyrate dehydrogenaseBeta-hydroxybutyrate dehydrogenaseNAD^+-β-hydroxybutyrate dehydrogenaseD-3-hydroxybutyrate dehydrogenaseBDH, HBD, BHBDH, β-hydroxybutyrate dehydrogenaseD-(−)-3-hydroxybutyrate dehydrogenaseHydroxybutyrate oxidoreductase, β-hydroxybutyric acid dehydrogenase, 3-D-hydroxybutyrate dehydrogenasePotentially: BDH2 (in mammals, refers to a related but distinct cytosolic enzyme with some similar activities; ambiguity exists)

Not applicable for approved therapeutics; experimental inhibitors would act as competitive inhibitors (blocking substrate or cofactor binding).