Regulation of spermidine acetyltransferase activity by phosphorylation and dephosphorylation.
Spermidine acetyltransferase activity is more than 10-fold higher in the pancreas of a 20-hr-fasted than in that of a fed chicken. The preparation of the fed bird inactivates the other. The effect is due to a thermolabile component of microsomes, and is also obtained with alkaline phosphatase. The inactivated preparation partially recovers its activity through phosphorylation catalyzed by a cAMP-dependent protein kinase. The results presented strongly suggest that spermidine acetyltransferase activity is regulated by phosphorylation and dephosphorylation.
D000123:Acetyltransferases / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002645:Chickens; D005215:Fasting; D006358:Hot Temperature; D008099:Liver / Q000201:enzymology; D008297:Male; D008861:Microsomes / Q000201:enzymology; D010179:Pancreas / Q000201:enzymology; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D000099228:Diamine N-Acetyltransferase
D000123:Acetyltransferases; D000469:Alkaline Phosphatase; D010710:Phosphates; D011494:Protein Kinases; D000099228:Diamine N-Acetyltransferase