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PERSPECTIVES AND SUMMARY Interest has been increasing during the last twenty years in the naturally occurring polyamines, putrescine (1,4-diaminobutane), spermidine, and spermine. 1 Their specific function is still obscure, but their ubiquitous distribution, their high concentration in cells, and the increase in the concentrations found in rapidly growing tissues have stimulated many investigations on these compounds. The biosynthetic pathways for putrescine, spermidine, and spermine are well established (Figure I). These pathways were first studied in pro karyotes, but, in general, the same biosynthetic steps have be:en found in eukaryotes. The enzymes involved in the specific steps have been purified and characterized from a variety of sources. Two of these enzymes are of particular interest : namely, ornithine decarboxylase and adenosyl methionine decarboxylase. Ornithine decarboxylase has a strikingly short turnover time in mammalian cells ( 10 min), and increases rapidly and dramatically after a variety of growth stimuli. Adenosylmethionine de carboxylase also has a relatively short half-life ('" 1-2 hr), and has the added interest that it contains covalently bound pyruvate as a cofactor instead of pyridoxal phosphate, the usual cofactor for decarboxylases. The short turnover times of these two enzymes presumably reflects the physiological importance of polyamines, and
Annual Review of Biochemistry – Annual Reviews
Published: Jul 1, 1984
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