Option a, b, c & d are the statements that accurately describe the structure of the pyruvate dehydrogenase (PDH) complex. Regulation arises from activation and deactivation.
The pyruvate dehydrogenase (PDH) complex in eukaryotes is tightly controlled by the enzymes pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP).
Multiple copies of the pyruvate dehydrogenase (E1) and the di-hydrolipoyl dehydrogenase (E3) in eukaryotes bind exclusively to the surface of the complex E2's core (dihydrolipoyl transacetylase).
The multidomain structure of dihydrolipoyl transacetylases complex is unique and consists of three lipoyl domains, an interaction domain, and a catalytic domain. The form of the arrangement of dihydrolipoyl transacetylase enzymes might be cubic or dodecahedral.
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