Heat activation of rat epididymal fat tissue acetyl-coa carboxylase is due to dephosphorylation by its endogenous phosphatase.
Acetyl-CoA carboxylase from rat epididymal fat tissue is activated by incubation at 30 C in the absence of citrate or metal ions. This activation is accompanied by a corresponding loss of 32P from the labeled enzyme, and it is not blocked by the heat-stable phosphorylase phosphatase inhibitor proteins from rabbit muscle. We have succeeded in separating an activity which activates and dephosphorylates acetyl-CoA carboxylase from the carboxylase using polyethylene glycol-6000. These results suggest that the temperature-dependent activation of acetyl-CoA carboxylase in crude or partially purified preparations results from dephosphorylation of the carboxylase by bound phosphatase.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D004789:Enzyme Activation; D006358:Hot Temperature; D008025:Ligases / Q000378:metabolism*; D008297:Male; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010758:Phosphorus / Q000378:metabolism; D010765:Phosphorylase Phosphatase / Q000037:antagonists & inhibitors; D051381:Rats
D010758:Phosphorus; C028732:acetyl CoA carboxylase phosphatase; D010749:Phosphoprotein Phosphatases; D010765:Phosphorylase Phosphatase; D008025:Ligases; D000103:Acetyl-CoA Carboxylase