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The effect of phosphorylation on pyruvate dehydrogenase
Author(s) -
Lioubov G. Korotchkina,
Ljudmila S. Khailova,
С. Е. Северин
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)00382-j
Subject(s) - pyruvate dehydrogenase complex , phosphorylation , pyruvate decarboxylation , pyruvate dehydrogenase kinase , chemistry , oxidative phosphorylation , dihydrolipoyl transacetylase , biochemistry , pyruvate dehydrogenase phosphatase , substrate (aquarium) , active site , pkm2 , pyruvate kinase , enzyme , biology , glycolysis , ecology
Phosphorylation of the pyruvate dehydrogenase component (E1) of the muscle pyruvate dehydrogenase complex (PDC) by E1‐kinase inhibits substrate conversion both in oxidative and non‐oxidative reactions. Circular dichroism spectra were used to monitor the effect of phosphorylation on the following stages of the process: holoform formation from apo‐E1 and thiamine pyrophosphate (TPP), substrate binding and active site deacetylation. It has been shown that phosphorylation of E1 reduces its affinity for TPP and prevents holo‐E1 interaction with pyruvate. Phosphorylated and dephosphorylated PDC convert 2‐hydroxyethyl‐TPP in similar ways involving half of their active sites; all active sites of E1 function in the presence of deacetylating agents. The data obtained suggest that the phosphorylation and substrate binding sites interact with each other.