Matsui I, Otani S, Kamei M, Morisawa S
FEBS Lett. 1982 Dec 13;150(1):211-3. doi: 10.1016/0014-5793(82)81336-7.
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.
在植物血凝素刺激的牛淋巴细胞提取物中的亚精胺N1 - 乙酰基转移酶，经与碱性磷酸酶预孵育后会失活。加入焦磷酸可完全抑制磷酸酶对乙酰化酶的失活作用。这些结果表明，多胺生物降解途径中的限速酶——亚精胺N1 - 乙酰基转移酶会因去磷酸化而失活。在大肠杆菌提取物中也观察到了碱性磷酸酶对乙酰化酶的类似作用。该乙酰化酶具有快速的周转速率，酶活性的快速丧失可能在一定程度上受共价修饰调控。
