EC Number |
Posttranslational Modification |
Reference |
---|
2.3.3.8 | phosphoprotein |
- |
703014, 735902 |
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 |
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 | 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 | 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 |
phosphorylation occurs on a His residue at the active site |
488209 |
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 |