Structural analysis of serine peptidase for construction of screening tool for novel biologically active substances
| Project/Area Number |
26450124
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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 | Tottori University |
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Principal Investigator |
Arima Jiro 鳥取大学, 農学部, 准教授 (80393411)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | アミノリシス / D体特異的アミノ酸アミド加水分解酵素 / 結晶構造解析 / 基質結合部位 / アシル受容体 / ペプチド結合形成反応 / 副反応 / 立体構造 / family S12ペプチダーゼ / 立体構造解析 / ペプチド結合形成 |
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| Outline of Final Research Achievements |
Serine peptidases that exhibit the catalytic ability of “aminolysis” are capable of utilizing biocatalyst for peptide synthesis. Therefore, such enzymes are considered to be useful as screening tool for novel biologically active substances. To clarify the mechanism of aminolysis function of D-stereospecific amino acid amide hydrolase (DAH) that exhibits high aminolysis function, the crystal structure of the enzyme was determined at a resolution of 1.6 angstrom. DAH possesses a large cavity that leads to the catalytic center, and there is a small pocked close to the catalytic center. By substitution of the residues that constitute the catalytic pocket, we found that the structural modification of Ile338 enhanced the aminolytic ability and were broaden the acyl acceptor specificity. The modification of pocket shape by the mutation is considered to be related to the increase in aminolysis activity of DAH
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Report
(4 results)
Research Products
(13 results)
