Neo-human-type oligosaccharide that imitates sialylation developed by structural analysis of fission yeast pyruvyltransferase Pvg1p
| Project/Area Number |
26292054
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
Takegawa Kaoru 九州大学, (連合)農学研究科(研究院), 教授 (50197282)
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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 |
¥16,510,000 (Direct Cost: ¥12,700,000、Indirect Cost: ¥3,810,000)
Fiscal Year 2016: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
Fiscal Year 2015: ¥6,760,000 (Direct Cost: ¥5,200,000、Indirect Cost: ¥1,560,000)
Fiscal Year 2014: ¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
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| Keywords | 分裂酵母 / 糖タンパク質 / シアル酸 / ピルビン酸 / 糖鎖工学 / 酸性糖鎖 / バイオテクノロジー / 微生物 / ピルビン酸含有糖鎖 / N-結合型糖鎖 |
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| Outline of Final Research Achievements |
Pyruvylation onto the terminus of oligosaccharide, widely seen from prokaryote to eukaryote, confers negative charges on the cell surface and seems to be functionally similar to sialylation, which is found at the end of human-type complex oligosaccharide. However, detailed molecular mechanisms underlying pyruvylation have not been clarified well. We first determined the crystal structure of fission yeast pyruvyltransferase Pvg1p. By combining molecular modeling with mutational analysis of active site residues, we obtained a Pvg1p mutant (Pvg1pH168C) that efficiently transferred pyruvyl moiety onto a human-type complex glycopeptide. The resultant pyruvylated human-type complex glycopeptide recognized similar lectins on lectin arrays as the α2,6-sialyl glycopeptides. This newly-generated pyruvylation of human-type complex oligosaccharides would provide a novel method for glyco-bioengineering.
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Report
(4 results)
Research Products
(32 results)
