EC Number   |
Posttranslational Modification |
Reference  |
|---|
    1.2.4.1 | more |
not regulated by phosphorylation/dephosphorylation |
348919, 348968 |
| 1.2.4.1 | proteolytic modification |
cleavage of 29 amino acid long leader peptide from alpha subunit suggested from deduced protein sequence |
348923 |
| 1.2.4.1 | side-chain modification |
inactivated by phosphorylation |
348935, 348936 |
| 1.2.4.1 | more |
enzyme from chloroplast is not regulated by phosphorylation/dephosphorylation |
348936 |
| 1.2.4.1 | side-chain modification |
- |
348983 |
| 1.2.4.1 | side-chain modification |
phosphorylation of recombinant alpha2,beta2 tetramer, 3.25 phosphoryl groups per mol tetramer are incorporated, 50% phosphorylation within 10 min, only the alpha subunit is phosphorylated |
348983 |
| 1.2.4.1 | side-chain modification |
addition of pyruvate decreases enzyme phosphyrylation and inactivation, more than 2 mol phosphate are incorporated per tetramer, modification of arginine residues by 2,3-butanedione decreases activity and prevents phosphorylation, suggesting that substrate binding sites and regulatory sites are close together |
348984 |
| 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 | 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 |
| 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 |
