Molecular basis for oligosaccharide epimerases and their related enzymes.
Project/Area Number |
26850059
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Applied biochemistry
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Research Institution | Hokkaido University |
Principal Investigator |
SABURI Wataru 北海道大学, (連合)農学研究科(研究院), 助教 (00598089)
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Project Period (FY) |
2014-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | セロビオース2-エピメラーゼ / エピメラーゼ / イソメラーゼ / オリゴ糖 / 部位特異的変異 / 基質特異性 / 反応特異性 |
Outline of Final Research Achievements |
Cellobiose 2-epimerase (CE) epimerizes the reducing end glucose residue of beta1-4 disaccharides to mannose residue. It shares the catalytic domain and site structures with other monosaccharide isomerases/epimerases. In this study, structure-function relationship of these enzymes was analyzed. Important amino acid residues for high selectivity for disaccharides in Rhodothermus marines CE were determined through site-directed mutation. Slight isomerization activity was observed in R. marines CE, and important structure for isomerase activity was determined based on the comparison of the structures between R. marines and Cardicellulosiruptor saccharolyticus CEs. A novel enzyme acting on mannose was found from function unknown proteins.
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Report
(3 results)
Research Products
(31 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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