1.
FEBS Lett
; 394(1): 96-8, 1996 Sep 23.
Article
in English
| MEDLINE
| ID: mdl-8925937
ABSTRACT
The mechanism of regulatory phosphorylation of the pyruvate dehydrogenase component (E1) of muscle pyruvate dehydrogenase complex was studied. Chemical modification of the arginine residues essential for substrate binding was shown to prevent incorporation of 32P from [gamma-32P]ATP into E1 catalyzed by kinase and to exclude completely the interaction of holo-E1 with pyruvate. It is proposed that negatively charged phosphoseryl residues may compete with pyruvate for the active site arginine and thereby block the substrate binding.