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Acanthamoeba culbertsoni, the free living pathogenic amoeba responsible for fatal meningoencephalitis, contains an S-adenosylmethionine decarboxylase (EC 4.1.1.50) which is strongly activated by putrescine and to a lesser extent by cadaverine; spermidine, spermine, diaminopropane and 1,6-diaminohexane are inactive. Methylglyoxal bis-(guanylhydrazone) competitively inhibited the enzyme with a Ki value of 123 microM. The enzyme was strongly inhibited by berenil (Ki = 0.5 microM) and to a lesser extent by pentamidine. The putrescine-activated enzyme is inhibited by MgCl2. The apparent molecular weight of 110,000 and its enzymatic properties indicate that the enzyme has characteristics intermediate between the bacterial and eukaryotic S-adenosylmethionine decarboxylases.
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