Investigating the result for emergence of flexible enzyme stereospecificity
Project/Area Number |
24570247
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Evolutionary biology
|
Research Institution | University of Tsukuba |
Principal Investigator |
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
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)
|
Keywords | トリプトファナーゼ / D-セリン / リン酸トリアンモニウム / ホモキラリティーの起原 / D-セリン / リン酸アンモニウム / 立体選択性 / リン酸3アンモニウム(TAP) / 光学分割 / DL-セリン |
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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Report
(4 results)
Research Products
(11 results)