Some Properties of the Arginine Decarboxylase in Vicia faba Leaves

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概要

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• Growth of Vicia faba seedlings is accompanied by a rapid increase in arginirie decarboxylase (EC 4.1.1.19) in the leaves and epicotyl. Increased enzyme activity was observed under saline conditions in the presence of NaCl and with osmotic stress by mannitol. The partially purified enzyme (about 86-fold) readily decarboxylated L-arginine, while D-arginine, L-homoarginine, L-ornithine and L-lysine were decarboxylated very slowly, and L-citrulline and L-glutamic acid were not decarboxylated. The K_m value was 5.8 × 10^<-4> M for L-arginine. The optimal pH and temperature for activity were 8.5 and 45℃, respectively. p-Chloromercuribenzoate and N-ethylmaleimide were effective inhibitors of the enzyme. Inhibition by spermidine, putrescine and agmatine suggested a possible feed-back mechanism in the pathway of polyamine biosynthesis.

• 日本植物生理学会の論文

著者

• Matsuda Hitoshi

  Science Education Institute Of Osaka Prefecture

関連論文

• Some Properties of the Arginine Decarboxylase in Vicia faba Leaves
• Purification and Properties of the Diamine Oxidase from Vicia faba Leaves
• Some properties of the amine oxidase in Vicia faba seedlings

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