Abstract
S-Adenosylmethionine decarboxylase (EC 4.1.1.50) has been purified 500-fold in 30% yield from the extract of etiolated corn seedlings (cv. Golden Crossbantam Bell). This preparation had a molecular weight of approximately 25,000. The K(m) value was 5 micromolar for S-adenosylmethionine. Methylglyoxal bis(guanylhydrazone), hydroxylamine, and sulfhydryl reagents (such as p-hydroxymercuriphenylsulfonate and N-ethylmaleimide) were effective inhibitors of this enzyme. Germination of corn seed was accompanied by a rapid increase in enzyme activity and maximum activity occurred in 5-day-old seedlings.