115(P-64) 植物二次代謝産物の二糖配糖体を特異的に加水分解するジグリコシダーゼの解析(ポスター発表の部)

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A β-primeverosidase from tea plants (Camellia sinensis) is a unique disaccharide-specific diglycosidase, which hydrolyses aroma precursors of β-primeverosides (6-O-β-D-xylopyranosyl-β-D-glucopyranosides) to liberate a primeverose unit and various aroma compounds. Recently we reported the purification and cloning of β-primeverosidase from tea plants. β-Primeverosidase is classified in glycosyl hydrolase family 1, in which many β-glucosidases from various plants are also present. In addition to β-primeverosidase, various kinds of disaccharide-specific diglycosidases such as β-acuminosidase, β-vicianase, β-rutinosidase, etc. are thought to be present in a wide range of plant kingdom. The purpose of this study is to investigate these diglycosidases from chemical, biochemical as well as physiological points of view. The cDNA coding for another diglycosidase (furcatin hydrolase), which hydrolyzes p-allylphenyl β-acuminoside, has been isolated from Viburnum fitrcatum. Furthermore, we have succeeded in the purification and cloning of the third diglycosidase (vicianin hydrolase) from immature seeds of Vicia angustifolia. These diglycosidases cluster together with β-primeverosidase in the phylogenetic tree of family 1 of plant β-glucosidases, suggesting that the disaccharide specific glycosidases form a new subfamily of family 1 glycosidase. The physiological functions of these diglycosidases in defense mechanism in plants as well as the evolution of the diglycosidases in relation to the presence of disaccharide glycosides in some plants are discussed.
天然有機化合物討論会の論文
2004-10-01

115(P-64) 植物二次代謝産物の二糖配糖体を特異的に加水分解するジグリコシダーゼの解析(ポスター発表の部)

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