Structure-function relationship of an arabinofuranosidase which have strict substrate specificity
| Project/Area Number |
25450140
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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 | University of the Ryukyus (2014-2015)
National Agriculture and Food Research Organization (2013) |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 酵素利用学 / 糖質関連酵素 / アラビノフラノシダーゼ / 糖加水分解酵素ファミリー62 / アラビノキシラン / 糖加水分解酵素 / ヘミセルラーゼ / 糖加水分解酵素ファミリー６２ |
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| Outline of Final Research Achievements |
α-L-Arabinofuranosidase, which belongs to the glycoside hydrolase family 62 (GH62), hydrolyzes arabinoxylan but not arabinan or arabinogalactan. The crystal structures of several α-L-arabinofuranosidases have been determined, although the structures, catalytic mechanisms, and substrate specificities of GH62 enzymes remain unclear. To evaluate the substrate specificity of a GH62 enzyme, we determined the crystal structure of an α-L-arabinofuranosidase from Streptomyces coelicolor.
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Report
(4 results)
Research Products
(2 results)
