Inactivation of spermidine N 1‐acetyltransferase with alkaline phosphatase

FEBS Letters

Otani, Shuzo¹  Kamei, Masaharu¹  Matsui, Isao¹  Morisawa, Seiji¹ 

[1] Department of Biochemistry, Osaka City University Medical School, Asahimachi, Abenoku, Osaka 545, Japan

关键词: Acetyltransferase;    Spermidine;    Alkaline phosphatase;    Polyamine metabolism;    Lymphocyte;    Escherichia coli;   

DOI  :  10.1016/0014-5793(82)81336-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Spermidine N ¹-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 N ¹-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.

【 授权许可】

Unknown