Acetylation of Decarboxylated S-Adenosylmethionine by Mammalian Cells

Anthony E. Pegg, Rita S. Wechter, Richard S. Clark, Laurie Wiest, Bradley G. Erwin

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Decarboxylated S-adenosylmethionine was found to be a substrate for the nuclear acetyl-transferases that act on polyamines and on histones. The rate of acetylation of decarboxylated Sadenosylmethionine was more than twice that of spermidine at saturating substrate concentrations, and decarboxylated S-adenosylmethionine was an active inhibitor of the acetylation of histones by nuclear extracts from rat liver. The acetylation of decarboxylated S-adenosylmethionine occurred in vivo in SV-3T3 cells exposed to the ornithine decarboxylase inhibitor 2-(difluoromethyl)ornithine. The decline in putrescine and spermidine brought about by exposure to 2-(difluoromethyl)ornithine was found to be accompanied by a large rise in the content of both decarboxylated S-adenosylmethionine and acetylated decarboxylated S-adenosylmethionine. These results indicate that decarboxylated S-adenosylmethionine is metabolized not only in the well-known reactions in which it serves as an aminopropyl donor for polyamine biosynthesis but also by acetylation in reaction with acetyl coenzyme A. Furthermore, the inhibition of histone acetylation by decarboxylated S-adenosylmethionine could contribute to the biological effects brought about by inhibitors of ornithine decarboxylase.

Original languageEnglish (US)
Pages (from-to)379-384
Number of pages6
JournalBiochemistry
Volume25
Issue number2
DOIs
StatePublished - Jan 1986

All Science Journal Classification (ASJC) codes

  • Biochemistry

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