S-Adenosylmethionine decarboxylase

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

S-Adenosylmethionine decarboxylase is a key enzyme for the synthesis of polyamines in mammals, plants and many other species that use aminopropyltransferases for this pathway. It catalyses the formation of S-adenosyl-1-(methylthio)-3-propylamine (decarboxylated S-adenosylmethionine), which is used as the aminopropyl donor. This is the sole function of decarboxylated S-adenosylmethionine. Its content is therefore kept very low and is regulated by variation in the activity of S-adenosylmethionine decarboxylase according to the need for polyamine synthesis. All S-adenosylmethionine decarboxylases have a covalently bound pyruvate prosthetic group, which is essential for the decarboxylation reaction, and have similar structures, although they differ with respect to activation by cations, primary sequence and subunit composition. The present chapter describes these features, the mechanisms for autocatalytic generation of the pyruvate from a proenzyme precursor and for the decarboxylation reaction, and the available inhibitors of this enzyme, which have uses as anticancer and anti-trypanosomal agents. The intricate mechanisms for regulation of mammalian S-adenosylmethionine decarboxylase activity and content are also described.

Original languageEnglish (US)
Pages (from-to)25-45
Number of pages21
JournalEssays in biochemistry
Volume46
Issue number1
DOIs
StatePublished - Dec 1 2009

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Adenosylmethionine Decarboxylase
Decarboxylation
Polyamines
Pyruvic Acid
Spermidine Synthase
Propylamines
Enzyme Precursors
Mammals
Enzyme Inhibitors
Prosthetics
Cations
Chemical activation
Enzymes
Chemical analysis

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

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S-Adenosylmethionine decarboxylase. / Pegg, Anthony E.

In: Essays in biochemistry, Vol. 46, No. 1, 01.12.2009, p. 25-45.

Research output: Contribution to journalArticle

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