| Project/Area Number |
16H06847
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | Shizuoka University |
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Principal Investigator |
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| Research Collaborator |
PARK Enoch Y. 静岡大学, グリーン科学技術研究所, 教授
KATO Tatsuya 静岡大学, 農学部, 准教授
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| Project Period (FY) |
2016-08-26 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 糖鎖 / 糖転移酵素 / 糖タンパク質 / Ｎ結合型糖鎖 / 複合型糖鎖 / カイコ / N結合型糖鎖 / X線結晶構造解析 / N-アセチルグルコサミン |
|---|
| Outline of Final Research Achievements |
This study focuses on the structure-function relationship of N-acetylglucosaminyltransferase (GnTII) which is essential for complex-type N-glycan biosynthesis. We obtained recombinant GnTII enzymes from human and Bombyx mori using Escherichia coli and silkworm as hosts, and the enzymes expressed in silkworm showed higher activity than those in E. coli. The substrate specificity and enzymatic activity of B. mori GnTII were almost identical to those of human GnTII. Although B. mori GnTII was more highly N-glycosylated than human GnTII, enzymatic cleavage of N-glycans did not affect their activity and thermostability, indicating that N-glycans which were attached to the enzymes are not important for their activity and stability.
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