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Inhibition of ornithine decarboxylase and glutamic acid decarboxylase activities by phosphorylethanolamine and phosphorylcholine.

Authors
  • Gilad, G M
  • Gilad, V H
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Jul 18, 1984
Volume
122
Issue
1
Pages
277–282
Identifiers
PMID: 6743332
Source
Medline
License
Unknown

Abstract

Ornithine decarboxylase, which catalyzes the first step in polyamine biosynthesis, is rapidly and transiently increased in various tissues during growth and after various hormonal or noxious stimuli, prior to an elevation in choline kinase activity. Polyamines themselves have been demonstrated to activate choline kinase. The present study sought to determine the effect of phosphorylcholine, the product of the reaction catalyzed by choline kinase, on ornithine decarboxylase activity. The data demonstrate that ornithine decarboxylase activity. The data demonstrate that ornithine decarboxylase activity is inhibited by phosphorylcholine and more potently by the related compound phosphorylethanolamine. The inhibition by both compounds led to decreased affinity of partially purified ornithine decarboxylase for ornithine. The inhibition is not time dependent and reversible. Both compounds also inhibit glutamic acid decarboxylase activity. The results suggest that high intracellular levels of phosphorylethanolamine and phosphorylcholine can serve as natural inhibitors of decarboxylases.

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