Rat Branched Chain Alpha-Ketoacid Dehydrogenase Kinase (BCKDK) Protein

Background

Branched Chain Keto Acid Dehydrogenase Kinase (BCKDK) is a pivotal regulatory enzyme in the catabolism of branched-chain amino acids (BCAAs), including leucine, isoleucine, and valine, which are essential amino acids important for protein synthesis, energy production, and metabolic signaling. BCKDK functions by phosphorylating and inhibiting the activity of the branched-chain α-keto acid dehydrogenase (BCKD) complex, a key enzymatic complex responsible for the oxidative decarboxylation of branched-chain α-keto acids derived from BCAAs. This regulatory action of BCKDK prevents excessive degradation of BCAAs and maintains metabolic balance, particularly under conditions requiring the conservation of these amino acids. Dysregulation of BCKDK activity has been implicated in metabolic disorders such as maple syrup urine disease (MSUD), characterized by the accumulation of toxic levels of BCAAs and their corresponding keto acids. Additionally, mutations in the BCKDK gene have been linked to neurodevelopmental disorders and autism spectrum disorders due to altered amino acid metabolism. Given its critical role in amino acid homeostasis and metabolic signaling, BCKDK is a potential therapeutic target for treating metabolic diseases and conditions associated with BCAA dysregulation.