Enzymatic synthesis of oligosaccharides, polysaccharides, and glycosides
| Project/Area Number |
15H04484
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
Mori Haruhide 北海道大学, 農学研究院, 教授 (80241363)
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| Co-Investigator(Kenkyū-buntansha) |
佐分利 亘 北海道大学, 農学研究院, 助教 (00598089)
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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 |
¥17,550,000 (Direct Cost: ¥13,500,000、Indirect Cost: ¥4,050,000)
Fiscal Year 2017: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2016: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2015: ¥11,830,000 (Direct Cost: ¥9,100,000、Indirect Cost: ¥2,730,000)
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| Keywords | 糖質合成 / 酵素利用 / 糖ヌクレオチド / 糖転移酵素 / 酵素 |
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| Outline of Final Research Achievements |
Carbohydrate includes a wide variety of molecules because of the diversity of constituent monosaccharides, linkages, and degrees of polymerization. They are highly expected to contain functional compounds useful for human life. Therefore, various synthetic methods are required for synthesis of various saccharides. In this study, enzymatic conversion from highly abundant carbohydrates in nature was established with two types of enzymes: glycoside synthase and glycosyl transferase. In the method with synthase, sugar nucleotides, substrates for glycoside synthases, were provided from sucrose, and disaccharides were efficiently produced through the one-pot reactions. A new group of glycosyl transferases were found. The enzymes in it acted on maltooligosaccharides and catalyzed glucosyl transfer reactions.
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Report
(4 results)
Research Products
(20 results)
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[Journal Article] Structural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamilies2016
Author(s)
Ye, Y., Saburi, W., Odaka, R., Kato, K., Sakurai, N., Komoda, K., Nishimoto, M., Kitaoka, M., Mori, H., and Yao, M.
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Journal Title
FEBS Lett
Volume: 590
Issue: 6
Pages: 828-837
DOI
Related Report
Peer Reviewed
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[Journal Article] Structural analysis of the α-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism.2015
Author(s)
Shen X, Saburi W, Gai Z, Kato K, Ojima-Kato T, Yu J, Komoda K, Kido Y, Matsui H, Mori H, Yao M
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Journal Title
Acta Crystallogr. D Biol. Crystallogr.
Volume: 71
Issue: 6
Pages: 1382-1391
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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