Abstract
The biosyntheses of the essential polyamines spermidine and spermine are dependent on the activity of S-adenosylmethionine decarboxylase (AdoMetDC; EC 4.1.1.50). AdoMetDC catalyzes the conversion of S-adenosylmethionine (AdoMet) to S-adenosyl-5′-(3-methylthiopropylamine), otherwise known as decarboxylated AdoMet (dcAdoMet), which in turn donates its aminopropyl group to either putrescine for the synthesis of spermidine, or spermidine for the synthesis of spermine. The latter two reactions are catalyzed by the transferase enzymes, spermidine synthase and spermine synthase, respectively. In Saccharomyces cerevisiae, a null mutation in the SPE2 gene, encoding AdoMetDC, conveys an absolute requirement for spermidine or spermine for growth (1), and mouse blastocysts lacking a functional copy of the AdoMetDC gene die at the early stage of gastrulation unless supplied with spermidine (2). As well as being the substrate for AdoMetDC, AdoMet is involved in many other essential biochemical processes in cells and is regarded as the major methyl donor in reactions catalyzed by methyltransferases. However, dcAdoMet is unable to fulfil these other functions, so AdoMetDC activity commits AdoMet to a role in polyamine biosynthesis.
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Hanfrey, C. (2006). Regulation of S-Adenosylmethionine Decarboxylase. In: Wang, JY., Casero, R.A. (eds) Polyamine Cell Signaling. Humana Press. https://doi.org/10.1007/978-1-59745-145-1_26
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DOI: https://doi.org/10.1007/978-1-59745-145-1_26
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