EC Number |
Posttranslational Modification |
Reference |
---|
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 | more |
enzyme from chloroplast is not regulated by phosphorylation/dephosphorylation |
348936 |
1.2.4.1 | more |
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 |