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EC Number
Posttranslational Modification
Commentary
Reference
phosphoprotein
-
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
phosphoprotein
phosphorylation of the enzyme at Thr446, Ser450 and Ser454 is enhanced by glucagon, insulin, vasopressin and transforming growth factor beta1
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; phosphoprotein
side-chain modification
contains 2 mol phosphate per mol of tetramer; phosphoprotein; 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
side-chain modification
contains 2 mol phosphate per mol of tetramer; phosphoprotein; structural phosphate behaves as a serine phosphate
side-chain modification
histidine phosphorylation of ATP-citrate lyase is inhibited by vanadate; phosphoprotein
side-chain modification
maximum level of phosphorylation is 2 mol phosphate per mol of tetramer, phosphorylation can affect the activity of the enzyme; phosphoprotein
side-chain modification
phosphoprotein
side-chain modification
phosphoprotein; phosphorylation occurs on a His residue at the active site
Results 1 - 10 of 12 > >>