PRINCIPLES OF SYMMETRICAL ORGANIZATION FOR THE PYRUVATE-DEHYDROGENASECOMPLEX

The experimentally observed phenomenon of non-equimolarity for enzyme components, assembled into multienzyme complexes of the Zero acid dehy drogenases family, is structurally interpreted to predict the only pos sible stable symmetrical distribution of peripheral components on the complex core, To obey the equivalent neighboring, that is necessary fo r unique self-assembled structures, we should deduce discrete conforma tional states for core subunits, those with different affinity for per ipheral components. Two kinetically different types of substrate-inter mediate pathways through the lipoyl network of the mammalian pyruvate dehydrogenase complex follow from this structural theory, The theory p redicts unusual kinetic behavior for the multienzyme complex.