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Inactivation of spermidine N 1 ‐acetyltransferase with alkaline phosphatase
Author(s) -
Matsui Isao,
Otani Shuzo,
Kamei Masaharu,
Morisawa Seiji
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81336-7
Subject(s) - spermidine , alkaline phosphatase , biochemistry , dephosphorylation , enzyme , pyrophosphate , chemistry , phosphatase , acetyltransferase , escherichia coli , spermine , pyrophosphatases , microbiology and biotechnology , biology , acetylation , gene
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.