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Arginine and Ornithine Decarboxylases, the Polyamine Biosynthetic Enzymes of Mung Bean Seedlings
Arie Altman, Ra'anan Friedman and Nitsa Levin
Vol. 69, No. 4 (Apr., 1982), pp. 876-879
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/4267315
Page Count: 4
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General properties and relative activities of L-arginine decarboxylase (ADC) (EC 220.127.116.11) and L-ornithine decarboxylase (ODC) (EC 18.104.22.168), two important enzymes in putrescine and polyamine biosynthesis, were investigated in mung bean (Vigna radiata L.) tissues. Both activities increase linearly with increasing concentrations of crude enzyme, but the increase in ADC activity is considerably greater. The decarboxylation reaction is linear for up to 30 to 60 minutes, and both enzymes have a pH optimum of 7.2. α-Difluoromethyl-ornithine inhibits ODC activity of excised roots, while increasing ADC activity. High specific activity of both enzymes is detected in terminal buds and leaves, while root and hypocotyl activity is low. Different ADC-to-ODC activity ratios are found in various tissues of mung bean plants. Substantial increase in the activity of both enzymes is detected in incubated sections as compared with intact plants. A comparison of several plant species indicates a wide range of ADC-to-ODC activity ratio. It is suggested that both ADC and ODC are active in plant tissues and that their relative contribution to putrescine biosynthesis is dependent upon the type of tissue and growth process.
Plant Physiology © 1982 American Society of Plant Biologists (ASPB)