| Budget Amount *help |
¥18,590,000 (Direct Cost: ¥14,300,000、Indirect Cost: ¥4,290,000)
Fiscal Year 2018: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2017: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2016: ¥9,490,000 (Direct Cost: ¥7,300,000、Indirect Cost: ¥2,190,000)
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| Outline of Final Research Achievements |
Neutron crystallography of copper amine oxidase revealed that the cofactor TPQ has both enolate and keto forms on the basis of its protonation state. It is clear that both forms had a distorted ring structure unlike a planner one that has been believed to be taken. The present study also provide detail information for structural changes of the catalytic intermediates during the catalytic cycle. Structural changes, distortion, and fluctuations of the active-site residues and cofactor can control energy level of transition state so that the rate of enzyme-catalyzed reaction is accelerated.
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