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Polyamine Biosynthesis
EditPolyamine biosynthesis is the enzymatic production of small organic polycations containing multiple amino groups. The pathway forms putrescine and converts it into higher polyamines through successive aminopropyl-transfer reactions. Spermidine and spermine arise from addition of aminopropyl groups supplied by decarboxylated S-adenosylmethionine [1][2]. Biosynthetic enzyme expression, substrate supply, and feedback regulation are coordinated with polyamine degradation, uptake, and export to maintain intracellular pools [3]. Ornithine decarboxylase produces putrescine in a major biosynthetic route and is subject to targeted degradation mediated by antizyme [4]. The supply of ornithine and activated aminopropyl donors connects successive steps to broader amino acid and methionine metabolism. The resulting network connects amino acid metabolism with the synthesis and interconversion of putrescine, spermidine, and related polyamines [5].
References
- Robert A. Casero; Tracy Murray Stewart; Anthony E. Pegg; Polyamine Metabolism and Cancer: Treatments, Challenges and Opportunities. Nat. Rev. Cancer 2018, 18, 681-695. [CrossRef]
- Robert A. Casero; Laurence J. Marton; Targeting Polyamine Metabolism and Function in Cancer and Other Hyperproliferative Diseases. Nat. Rev. Drug Discov. 2007, 6, 373-390. [CrossRef]
- Olle Heby; Lo Persson; Molecular Genetics of Polyamine Synthesis in Eukaryotic Cells. Trends Biochem. Sci. 1990, 15, 153-158. [CrossRef]
- Philip Coffino; Regulation of Cellular Polyamines by Antizyme. Nat. Rev. Mol. Cell Biol. 2001, 2, 188-194. [CrossRef]
- Chaim Kahana; The Antizyme Family for Regulating Polyamines. J. Biol. Chem. 2018, 293, 18730-18735. [CrossRef]
