A tryptophan decarboxylase from cucumber seedlings

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Abstract
The formation of tryptamine from tryptophan by extracts of cucumber hypocotyls is mediated by a tryptophan decarboxylase. The enzyme requires pyridoxal-5′-phosphate, and the pH optimum of this enzyme is 7.0. The activity of the enzyme is inhibited by potassium cyanide, but not by sodium azide or sodium fluoride; indicating that this enzyme is a decarboxylase rather than a peroxidase. The removal of contaminating epiphytic bacteria does not significantly affect the enzyme activity, and preincubation of enzyme extracts in streptomycin is also without effect. Neither aerobic nor anaerobic cultures of internal bacteria which contaminate cucumber hypocotyb exhibit enzymic activity at pH 7.0.

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