Pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO 2 in the presence of NAD+ (1). Acetyl-CoA then goes into citric acid cycle to react with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis (1). The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and citric acid cycle and lipid metabolism (1). In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two types of subunits: alpha and beta. This enzyme catalyzes the removal of one carbon as CO 2 from pyruvate. Mutations in the alpha subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration and early death (2).
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