Phosphorylation of different sites of acetyl CoA carboxylase by ATP-citrate lyase kinase and cyclic AMP-dependent protein kinase.
Native acetyl CoA carboxylase was phosphorylated by catalytic subunit of cyclic AMP-dependent protein kinase and ATP-citrate lyase kinase to 1 and 0.5 mol/subunit respectively. Both protein kinases added together increased acetyl CoA carboxylase phosphorylation additively. Partial proteolysis of 32P-acetyl CoA carboxylase followed by electrophoretic analysis showed that the 32P-phosphopeptides generated from acetyl CoA carboxylase phosphorylated with lyase kinase were different from the peptides obtained from the enzyme phosphorylated by cyclic AMP-dependent protein kinase. Mapping of tryptic 32P-phosphopeptides by high performance liquid chromatography showed that the major phosphopeptides phosphorylated by ATP-citrate lyase kinase were different from the major phosphopeptides phosphorylated by cyclic AMP-dependent protein kinase. The results suggest that at least one different site on acetyl CoA carboxylase is preferentially phosphorylated by each protein kinase.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D011494:Protein Kinases; C032202:ATP-citrate lyase kinase; D014357:Trypsin; D008025:Ligases; D000103:Acetyl-CoA Carboxylase