Subunit binding in the pyruvate dehydrogenase complex from bovine kidney and heart

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Abstract
Binding of pyruvate dehydrogenase (E1) and dihydrolipoamide dehydrogenase (E3) to the isolated dihydrolipoamide acetyltransferase (E2) core of the pyruvate dehydrogenase complex from bovine heart and kidney was investigated with equilibrium, competitive binding and kinetic methods. E2, which consists of 60 subunits arranged with icosahedral 532 symmetry, apparently possesses 6 equivalent, noninteracting binding sites for E3 dimers. It is proposed that each E3 dimer extends across 2 of the 12 faces of the E2 pentagonal dodecahedron. The equilibrium constant (Kd) for dissociation of E3 from E2 is about 3 nM, and the dissociation rate constant is about 0.057 min-1. For E1, Kd is about 13 nM, and the dissociation rate constant is about 0.043 min-1. Extensive phosphorylation of E1 (about 3 phosphoryl groups per E1 tetramer) increases Kd to about 40 nM.

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