1.2.4.1	glycoprotein	the O-glycosylation of PDH E1alpha is involved in the regulation of the PDH activity	712851	
1.2.4.1	additional information	enzyme from chloroplast is not regulated by phosphorylation/dephosphorylation	348936	
1.2.4.1	additional information	not regulated by phosphorylation/dephosphorylation	348919, 348968	
1.2.4.1	phosphoprotein	during lactate consumption, component E1 subunuit alpha Ser293 and Ser300 phosphorylation levels are 33% higher compared to the phase of glucose excess. At the same time, the relative phosphorylation level of Ser232 increases steadily throughout the cultivation (66% increase overall)	762973	
1.2.4.1	phosphoprotein	enzyme is subject to regulation by phosphorylation at residues S232, S293, S300	759082	
1.2.4.1	phosphoprotein	mitochondrial proteins, Pkp2 (Ygl059wp) and Ppp2 (Ycr079wp), are engaged in the regulation of the pyruvate dehydrogenase complex by affecting the phosphorylation state of subunit Pda1	759464	
1.2.4.1	phosphoprotein	phosphorylation of the PDH E1alpha subunit by PDH kinase contributes to the suppression of PDH activity. Streptozotocin treatment causes a significant increase in the level of the phosphorylated PDH E1alpha subunit in the diabetic rat hearts	712851	
1.2.4.1	phosphoprotein	the enzyme, as pyruvate dehydrogenase multienzyme complex component E1alpha, becomes reversibly phosphorylated at 3 serine residues by specific pyruvate dehydrogenase kinases PDK1-4, and dephosphorylated by a specific pyruvate dehydrogenase phosphatase PDP-1 and to a lesser extant PDP-2, regulatory function, pyruvate oxidation is inhibited in phosphorylated state of E1alpha	654462	
1.2.4.1	phosphoprotein	the PDC is tightly regulated by reversible phosphorylation at three known phosphorylation sites on PDHE1a: Ser293, Ser300, and Ser232	710839	
1.2.4.1	phosphorylation	phosphorylation of Ser264 slows the preceding binding of substrate to the enzyme's active site via the substrate channel and the subsequent reductive acetylation of the E2 component	685160