Principles of symmetrical organization for the pyruvate dehydrogenase complex

FEBS Letters

Goldstein, Boris N.¹  Saifullin, Salavat R.²  Zakrzhevskaya, Dina T.¹ 

[1] Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region 142292, Russian Federation;Institute of Mathematical Problems of Biology, Russian Academy of Sciences, Pushchino, Moscow Region 142292, Russian Federation

关键词: Enzyme structural symmetry;    Kinetic mechanism;    2-Oxo acid dehydrogenase;   

DOI  :  10.1016/0014-5793(95)01057-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown