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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Matsui I,Otani S,Kamei M,Morisawa Sdoi
10.1016/0014-5793(82)81336-7subject
Has Abstractpub_date
1982-12-13 00:00:00pages
211-3issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(82)81336-7journal_volume
150pub_type
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