Inactivation of spermidine N1-acetyltransferase with alkaline phosphatase.

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 Lett

journal_title

FEBS letters

authors

Matsui I,Otani S,Kamei M,Morisawa S

doi

10.1016/0014-5793(82)81336-7

subject

Has Abstract

pub_date

1982-12-13 00:00:00

pages

211-3

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(82)81336-7

journal_volume

150

pub_type

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