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The **dihydrolipoyl acetyltransferase (E2)** core is the central catalytic component of the pyruvate dehydrogenase complex (PDC). It organizes and assembles the multi-enzyme complex, shuttles reaction intermediates between active sites via covalently attached lipoyl groups, and catalyzes the transfer of acetyl groups from hydroxyethyl-lipoamide to coenzyme A, forming acetyl-CoA. In mammals, E2 combines with the homologous but pseudocatalytic E3BP to form a dodecahedral or pseudoicosahedral core, serving as the scaffold for integration of the peripheral E1 (pyruvate decarboxylase) and E3 (dihydrolipoamide dehydrogenase) enzymes. This makes E2 central to metabolism and a regulatory node in energy homeostasis.
Activation of pyruvate dehydrogenase via inhibition of pyruvate dehydrogenase kinase increases PDHc activity (e.g., by dichloroacetate) Supplementation of cofactors (thiamine) to support enzymatic function
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