| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Outline of Final Research Achievements |
Generally speaking, D-amino acids are inert to enzyme. Tryptophanase with absolute enantioselectivity is also inactive on D-serine. However it conversely turns around to active substrate in the presence of concentrate triammoniumphosphate. This reaction is mysterious because enzyme enantioselectivity is absolutely constant in enzymological common sense. Thereby this research, Grant-in-Aid for Scientific Research (C), was programed to figure out its reaction mechanism. It turned out that the flexible enantioselectivity was ascribed to the process of enzyme-D-serine complex formation in the presence of triammonium phosphate.
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