Influence of the cavity structure of enzymic active sites on the selectivity for alcohol isomers from n-alkane
| Project/Area Number |
23760739
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Catalyst/Resource chemical process
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
MIYAJI Akimitsu 東京工業大学, 総合理工学研究科(研究院), 助教 (40452023)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 分子認識 / 生成物選択性 / 酵素反応 / 直鎖アルカン / アルコール異性体 / 触媒・化学プロセス / アルコール |
|---|
| Research Abstract |
Regio- and enantioelectivities for alcohol isomes from n-alkanes by soluble methane monooxygenase, particulate methane monooxygenase, ammonia monooxygenase, and cytochrome P450 BM-3 were measured for investigating the influence of cavity structure of enzymic active site on n-alkane recognition at the active site. From the selectivity, orientation of n-alkanes at the active site of enzymes was determined. According to the active site structure of the enzymes used here, we revealed that n-alkane recognition was dependent on the volume of active site cavity and the properties of amino acid residues composing the cavity.
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Report
(4 results)
Research Products
(21 results)
