CHANGES IN ACTIVITY OF SHIKIMATE : NADP OXIDOREDUCTASE IN RELATION TO LIGNIFICATION OF BAMBOO
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概要
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Shikimate : NADP oxidoreductase (5-dehydroshikimate reductase; EC 1.1.1.25) was extracted from immature bamboo and partially purified. 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 substrate were found to be 1.4×10^<-4>M and 2.0×10^<-4>M, respectively, at pH 8.0. No metal requirement could be demonstrated since little change in enzyme activity was observed on addition of ethylenediamine-tetraacetic acid (EDTA). On the other hand, the enzyme was potently inhibited by p-chloromercuribenzoic acid (PCMB). 5-Dehydroshikimate reductase was demonstrated to be widely distributed in 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, but after reaching maximal content in the part just below the top, it began to decrease toward lower parts of bamboo. The enzyme activity at the top was the highest and seemed to decrease toward the tissues of lower parts. However the fact that the activity was still maintained at a certain level even in the aged tissues suggests that 5-dehydroshikimate reductase might play a significant role for biosynthesis of lignin.
- 日本植物生理学会の論文
著者
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SHIMADA Mikio
Laboratory of Biochemical Control, Wood Research Institute, Kyoto University
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Shimada Mikio
Laboratory Of Biochemical Control Wood Research Institute Kyoto University
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Shimada Mikio
Laboratory Of Wood Chemistry Faculty Of Agriculture Gifu University
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Higuchi Takayoshi
Laboratory Of Wood Chemistry Faculty Of Agriculture Gifu University
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