PMID:6297970
| Citation |
Matsui, I, Otani, S, Kamei, M and Morisawa, S (1982) Inactivation of spermidine N1-acetyltransferase with alkaline phosphatase. FEBS Lett. 150:211-3 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Acetyltransferases/antagonists & inhibitors; Alkaline Phosphatase/metabolism; Animals; Cattle; Diphosphates/pharmacology; Dose-Response Relationship, Drug; Lymphocyte Activation; Phytohemagglutinins |
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