Principles of symmetrical organization for the pyruvate dehydrogenase complex.
The experimentally observed phenomenon of non-equimolarity for enzyme components, assembled into multienzyme complexes of the 2-oxo acid dehydrogenases family, is structurally interpreted to predict the only possible stable symmetrical distribution of peripheral components on the complex core. To obey the equivalent neighboring, that is necessary for unique self-assembled structures, we should deduce discrete conformational states for core subunits, those with different affinity for peripheral components. Two kinetically different types of substrate-intermediate pathways through the lipoyl network of the mammalian pyruvate dehydrogenase complex follow from this structural theory. The theory predicts unusual kinetic behavior for the multienzyme complex.
Goldstein
B N
BN
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.
Saifullin
S R
SR
Zakrzhevskaya
D T
DT
D000818:Animals; D007700:Kinetics; D011487:Protein Conformation; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000378:metabolism; D008063:Thioctic Acid / Q000031:analogs & derivatives / Q000378:metabolism
D011768:Pyruvate Dehydrogenase Complex; D008063:Thioctic Acid; C013091:lipoamide