| Project/Area Number |
15K07401
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Tokyo Denki University |
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Principal Investigator |
NATSUME Ryo 東京電機大学, 工学部, 教授 (60637651)
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| Co-Investigator(Renkei-kenkyūsha) |
KAWASAKI Hisashi 東京電機大学, 工学部, 教授 (90349788)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | βアミノ酸 / 光学分割 / アミノアシラーゼ / 結晶構造解析 / 構造機能相関 |
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| Outline of Final Research Achievements |
In order to reveal the structure-function relationship of beta-phenylalanine aminoacylase capable of enantio-pure (R)-beta phenylalanine production, in this study, recombinant expression, purification, crystallization, x-ray crystallographic analysis, biochemical analysis of beta-phenylalanine aminoacylases derived from two micro-organisms, Burkholderia sp. and Variovorax sp., were performed. The crystal structure of the Burkholderia enzyme was successfully determined at 2.1 angstrom resolution. The structure-function relationship analyses of the Burkholderia enzyme utilizing site-specific mutants are in progress. The Variovorax enzyme was crystallized and the diffraction images beyond 2.5 angstrom resolution were collected. However, the crystal structure of the Variovorax enzyme has not been determined, because all collected images were from twinned crystals. Biochemical analyses showed that the Variovorax enzyme has an absolute specificity for R-enantiomer substrate.
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