CHANGES IN ACTIVITY OF SHIKIMATE : NADP OXIDOREDUCTASE IN RELATION TO LIGNIFICATION OF BAMBOO

Shikimate : NADP oxidoreductase (5-dehydroshikimate reductase;EC 1.1.1.25[EC]) was extracted from immature bamboo and partiallypurified. The optimal pH of the enzyme was found to be 11.0.The enzyme was demonstrated to be NADP specific. Michaelis constants (Km) for NADP and shikimic acid as substratewere found to be 1.4 10^–4M and 2.0 10^–4M, respectively,at pH 8.0. No metal requirement could be demonstrated sincelittle change in enzyme activity was observed on addition ofethylenediamine-tetraacetic acid (EDTA). On the other hand,the enzyme was potently inhibited by p-chloromercuribenzoicacid (PCMB). 5-Dehydroshikimate reductase was demonstrated to be widely distributedin woody plants such as bamboo, udo (Aralia cordata), asparagus(Asparagus officinalis) and tulip tree (Liriodendron tulipifera)as well as other higher plants. Shikimic acid content was comparatively low at the top, butafter reaching maximal content in the part just below the top,it began to decrease toward lower parts of bamboo. The enzymeactivity at the top was the highest and seemed to decrease towardthe tissues of lower parts. However the fact that the activitywas still maintained at a certain level even in the aged tissuessuggests that 5-dehydroshikimate reductase might play a significantrole for biosynthesis of lignin. (Received September 5, 1966; )