Inhibition of S-adenosylmethionine decarboxylase from rat liver by synthetic decarboxylated S-adenosylmethionine and its analogs.

Abstract

Synthetic decarboxylated S-adenosylmethionine and 6 analogs were tested in a decarboxylating system based on rat liver S-adenosylmethionine decarboxylase. All the compounds inhibited the putrescine-activated decarboxylase activity, and were competitive with respect to S-adenosylmethionine. Among the compounds tested, S-5''-deoxyadenosyl-(5'')-2-methylthioethylamine was the most potent inhibitor. The Ki [inhibition constant] value of the inhibitor was 7 times lower than that of decarboxylated S-adenosylmethionine.