EC Number   |
Posttranslational Modification |
Reference |
|---|
   1.2.1.104 | more |
not regulated by phosphorylation/dephosphorylation |
348914, 348931, 348947, 348958, 348971, 348977, 348986 |
| 1.2.1.104 | phosphoprotein |
brain aging is associated with a decrease of pyruvate dehydrogenase activity upon phosphorylation of the E1alpha subunit. Decreases in activity of about 25% and about 45% are found in mitochondria from 14- and 24-months old rats, respectively. The pyruvate dehydrogenase kinase-2-dependent inhibition of PDH activity amounts to about 20%, 43%, and 49% at 6, 14, and 24 months of age, respectively |
712006 |
| 1.2.1.104 | phosphoprotein |
component E1 is subject to regulation by phosphorylation at residues S232, S293, S300 |
759082 |
| 1.2.1.104 | 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 |
| 1.2.1.104 | 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 |
| 1.2.1.104 | phosphoprotein |
PDH activity is inhibited by the phosphorylation of its E1alpha1 subunit |
713120 |
| 1.2.1.104 | phosphoprotein |
regulation of activity by pyruvate dehydrogenase kinase isoenzymes. PDK2 has the highest activity for site S264 of PDH2, PDK3 has higher activity for site S271 than for site S264, and only PDK1 can phosphorylate site S203 |
674778 |
| 1.2.1.104 | phosphoprotein |
regulation of pyruvate dehydrogenase complex activity through reversible phosphorylation |
656612 |
| 1.2.1.104 | side-chain modification |
- |
348910, 348914, 348957, 94884 |
| 1.2.1.104 | side-chain modification |
inactivated by phosphorylation |
348910, 348913, 348914, 348954, 348973, 348989 |
