Premium
Principles of symmetrical organization for the pyruvate dehydrogenase complex
Author(s) -
Goldstein Boris N.,
Saifullin Salavat R.,
Zakrzhevskaya Dina T.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01057-l
Subject(s) - pyruvate dehydrogenase complex , chemistry , l lactate dehydrogenase , biochemistry , dihydrolipoyl transacetylase , lactate dehydrogenase , pyruvate decarboxylation , enzyme
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.