In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 188.8.131.52 and 184.108.40.206, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progressive increase in the amount of antizyme 1 and antizyme 2 occurs. The amino acid compositions of antizymes 1 and 2 show them to be basic proteins; antizyme 1 has an amino acid composition similar to that of the E. coli histone-like protein HU and of the eukaryotic histone H2B; antizyme 2 is characterized by an unusually high arginine content. We find these proteins to be specific inhibitors of both the biosynthetic ornithine decarboxylase and the biosynthetic arginine decarboxylase. They do not inhibit the corresponding biodegradative ornithine and arginine decarboxylases, nor do they inhibit lysine decarboxylase or S-adenosylmethionine decarboxylase. These properties of the antizymes favor their function in the regulation of polyamine biosynthesis in E. coli. The ability of the purified antizymes to inhibit the ornithine and arginine decarboxylases is stabilized in acidic buffers and is lost upon prolonged exposure to solutions at neutral or basic pH.
|Original language||English (US)|
|Number of pages||4|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Sep 1983|
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