Abstract
A pyridoxal phosphate-dependent tryptophan decarboxylase has been purified 20-fold from seedlings of Phalaris tuberosa. The enzyme activity of the seedlings reached a maximum after 4 days. The enzyme activity is maximal at pH 7·6 and could be demonstrated either by the production of 14C-tryptamine from methylene 14C- l-tryptophan or of 14CO 2 from carboxyl- 14C- l-tryptophan. d-tryptophan was not a substrate but 5-hydroxy- 14C-tryptophan was. The decarboxylation was inhibited at concentrations of 0·1 mM by a number of indole derivatives including N, N-dimethyltryptamine, one of the two major alkaloids produced by the plant. The second alkaloid, 5-methoxy- N, N-dimethyltryptamine did not inhibit at this concentration. A possible role of this enzyme in alkaloid biosynthesis is discussed.
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