The eukaryotic Pyruvate Dehydrogenase Complex (PDC) is a multi-enzyme complex organized around a dodecahedral core formed by the dihydrolipoyl transacetylase (E2) component. To this core, multiple copies of the thiamin diphosphate-dependent pyruvate dehydrogenase (E1) component, the FAD-containing dihydrolipoamide dehydrogenase (E3) component, and one to two copies each of pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP, which comprises a catalytic and regulatory subunit) are tethered via non-covalent interactions. The PDC functions in the mitochondrial matrix to catalyze the oxidative decarboxylation of pyruvate to produce acetyl-CoA and NADH and as such is the gate-keeper enzyme that links glycolysis to the Krebs cycle and lipogenic pathways. (Adapted from PMID:19081061.)

pyruvate dehydrogenase system (1.2.1.104)