| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Outline of Final Research Achievements |
This study is to elucidate the catalytic mechanism and substrate recognition for beta-amyrin synthase. Studies on the triterpene cyclase has encountered a difficulty, becaseu of the unstability of the membrane-bound protein. We developted a new strategy to evaluate the enzyme activity in vivo by estimating the expression amount of the cyclase enzyme and the quantities of triterpene produced. By this procedure, we identified many active site residues, especailly, Trp257 residue works not only to stabilize the cationic intermediate via cation-pi interaction, but also to tightly hold the Methyl-30 of the substrate via CH-pi interaction. In the substrate analog experiments revealed the importance of methyl-30 for the normal folding conformation leading to beta-amyrin skeleton.
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