Arginine decarboxylase is a component activity of the multifunctional.

ABSTRACT

A homogenous preparation of putrescine synthase, the versatile multifunctional enzyme involved in agmatine→putrescine conversion in Cucumis sativus was found to catalyze enzymatic decarboxylation of arginine also. Similarly, the purified arginine decarboxylase mediated the component as well as the complete set of coupled reactions harboured by putrescine synthase. Both the enzyme preparations exhibited identical electrophoretic and chromatographic behaviour and were immunologically indistinguishable. All the enzymic activities are stabilized concurrently by feeding arginine to the intact seedlings. Therefore, it is concluded that the multifunctional putrescine synthase in Cucumis sativus seedlings also harbours arginine decarboxylase activity unlike its counterpart in Lathyrus sativus.