Abstract
Summary Baker's yeast (Saccharomyces cerevisiae) is a rich source of two enzymes responsible for the synthesis of spermidine: (i) S-adenosyl methionine decarboxylase, and (ii) spermidine synthase, which catalyzes the synthesis of spermidine from decarboxylated S-adenosyl methionine and putrescine. The yeast S-adenosyl methionine decarboxylase has been purified about 400-fold, and largely separated from the bulk of spermidine synthase activity present in the crude yeast extracts. In marked contrast to the enzyme from E.coli , the yeast S-adenosyl methionine decarboxylase resembles a similar enzyme previously described in rat ventral prostate insofar as it is specifically enhanced by putrescine, and does not require Mg++ or any other dissociable metal cofactor. Some differences in the enzymic decarboxylation of S-adenosyl methionine by prostate, yeast, and E.coli are briefly discussed.
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