EC Number   |
Posttranslational Modification  |
Reference |
|---|
    2.3.3.8 | acetylation |
human knee osteoarthritis chondrocytes exhibit increased ACLY activation (assessed by Ser-455 phosphorylation), associated with increased H3K9 and H3K27 acetylation |
757200 |
| 2.3.3.8 | acetylation |
the enzyme is activated by acetylation at lysine residues 540, 546, and 554 |
756333 |
| 2.3.3.8 | phosphoprotein |
- |
703014, 735902 |
| 2.3.3.8 | phosphoprotein |
human knee osteoarthritis chondrocytes exhibit increased ACLY activation (assessed by Ser-455 phosphorylation), associated with increased H3K9 and H3K27 acetylation |
757200 |
| 2.3.3.8 | phosphoprotein |
phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Cyclic AMP-dependent protein kinase catalyzes the incorporation of 1 mol of phosphate per mol of enzyme homotetramer, and glycogen synthase kinase-3 incorporated an additional 2 mol of phosphate into the phosphorylated protein |
488221 |
| 2.3.3.8 | phosphoprotein |
phosphorylation of the enzyme at Thr446, Ser450 and Ser454 is enhanced by glucagon, insulin, vasopressin and transforming growth factor beta1 |
718760 |
| 2.3.3.8 | phosphoprotein |
the enzyme is activated by phosphorylation |
756333 |
| 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 |
contains 2 mol phosphate per mol of tetramer |
488191, 488199 |
| 2.3.3.8 | side-chain modification |
histidine phosphorylation of ATP-citrate lyase is inhibited by vanadate |
488210 |
