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Principles of symmetrical organization for the pyruvate dehydrogenase complex

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
373
Issue
3
Identifiers
DOI: 10.1016/0014-5793(95)01057-l
Keywords
  • Enzyme Structural Symmetry
  • Kinetic Mechanism
  • 2-Oxo Acid Dehydrogenase
Disciplines
  • Biology

Abstract

Abstract 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.

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