Phosphorylation of proteolytically-nicked rat hepatic acetyl-CoA carboxylase.
A partially-purified preparation of acetyl-CoA carboxylase was not inactivated by ATP and Mg2+ although it was phosphorylated. SDS gel electrophoresis of the phosphorylated enzyme showed phosphopeptides migrating at 140 and 40 K along with the 250 K native subunit. Phosphorylation by the catalytic subunit of cAMP-dependent protein kinase further phosphorylated an additional 120 K phosphopeptide. Neither cAMP-independent phosphorylation nor the cAMP-dependent phosphorylation of the enzyme resulted in a significant decrease in activity.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000818:Animals; D002850:Chromatography, Gel; D000242:Cyclic AMP / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D007163:Immunosorbent Techniques; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008297:Male; D010447:Peptide Hydrolases / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D000242:Cyclic AMP; D011494:Protein Kinases; D010447:Peptide Hydrolases; D008025:Ligases; D000103:Acetyl-CoA Carboxylase