EC Number   |
Posttranslational Modification |
Reference  |
|---|
    2.3.3.8 | side-chain modification |
maximum level of phosphorylation is 2 mol phosphate per mol of tetramer, phosphorylation can affect the activity of the enzyme |
488184 |
| 2.3.3.8 | side-chain modification |
phosphoprotein |
488184, 488191, 488195, 488199, 488205, 488209, 488210 |
| 2.3.3.8 | side-chain modification |
contains 2 mol phosphate per mol of tetramer |
488191, 488199 |
| 2.3.3.8 | side-chain modification |
regulation of the enzyme by reversible phosphorylation. The enzyme which has been phosphorylated by cyclic-AMP-dependent protein kinase, can be completely dephosphorylated by incubation with either protein phosphatase 1 or protein phosphatase 2 |
488191 |
| 2.3.3.8 | side-chain modification |
structural phosphate behaves as a serine phosphate |
488199 |
| 2.3.3.8 | side-chain modification |
citrate lyase phosphorylation by cAMP-dependent protein kinase or this kinase plus glycogen synthase kinase-3 decreases the maximal velocity whereas the apparent Km for citrate is unchanged |
488205 |
| 2.3.3.8 | side-chain modification |
phosphorylation occurs on a His residue at the active site |
488209 |
| 2.3.3.8 | side-chain modification |
histidine phosphorylation of ATP-citrate lyase is inhibited by vanadate |
488210 |
| 2.3.3.8 | side-chain modification |
the phosphorylation occurs by a direct transfer of a phosphoryl group from the catalytic His of nucleoside diphosphate kinase to a His on the ATP-citrate lyase |
488214 |
| 2.3.3.8 | side-chain modification |
phosphorylation on Ser residues by a cytosolic kinase, insulin enhances the Ser phosphorylation by 2-3-fold |
488215 |
