The effect of phosphorylation on pyruvate dehydrogenase.
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.[1]References
- The effect of phosphorylation on pyruvate dehydrogenase. Korotchkina, L.G., Khailova, L.S., Severin, S.E. FEBS Lett. (1995) [Pubmed]
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