3-Hydroxybutyrate Dehydrogenase 1 (BDH1)

DBH; SDR9C1; D-beta-Hydroxybutyrate Dehydrogenase,Mitochondrial; Short Chain Dehydrogenase/Reductase Family 9C,Member 1

3-Hydroxybutyrate Dehydrogenase 1 (BDH1)
BDH is a mitochondrial membrane enzyme with an absolute and specific requirement for phosphatidylcholine, which acts as an allosteric activator of BDH enzymatic activity. BDH has served as a prototype for lipid-requiring enzymes. Sequence analysis revealed that the first two-thirds of the BDH protein is homologous to short-chain alcohol dehydrogenases (SCADHs), with the homology encompassing the putative coenzyme-binding and active sites of the SCADHs; this region of BDH also has the predicted secondary structure motif of alternating alpha-helices and beta-sheets that is characteristic of SCADHs. The authors suggested that the remainder of the BDH protein contains elements that form the substrate- and lipid-binding sites. Northern blot analysis revealed that BDH is expressed in rabbit heart tissue.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)