Inactivation of spermidine N1-acetyltransferase with alkaline phosphatase.
Spermidine N1-acetyltransferase in an extract from phytohemagglutinin-stimulated bovine lymphocytes was inactivated by preincubation with alkaline phosphatase. Inactivation of the acetylase with the phosphatase was totally inhibited by addition of pyrophosphate. These results suggest that spermidine N1-acetyltransferase, the rate-limiting enzyme in the biodegradative pathway of polyamines, is inactivated by dephosphorylation. A similar effect of alkaline phosphatase on the acetylase in an extract from Escherichia coli was also observed. The acetylase has a rapid rate of turnover and the rapid loss of the enzyme activity may be to some extent regulated by the covalent modification.
D000123:Acetyltransferases / Q000037:antagonists & inhibitors*; D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D011756:Diphosphates / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D008213:Lymphocyte Activation; D010835:Phytohemagglutinins; D000099228:Diamine N-Acetyltransferase
D000123:Acetyltransferases; D000469:Alkaline Phosphatase; D011756:Diphosphates; D010835:Phytohemagglutinins; D000099228:Diamine N-Acetyltransferase