| Project/Area Number |
10306007
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| Research Category |
Grant-in-Aid for Scientific Research (A).
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
KUMAGAI Hidehiko Kyoto University, Graduate School of Biostudies, Professor, 生命科学研究科, 教授 (70027192)
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| Co-Investigator(Kenkyū-buntansha) |
TAMAKI Hisanori Kyoto University, Graduate School of Biostudies, Assistant, 生命科学研究科, 助手 (20212045)
SUZUKI Hideyuki Kyoto University, Graduate School of Biostudies, Associate Professor, 生命科学研究科, 助教授 (10202136)
YAMAMOTO Kenji Kyoto University, Graduate School of Biostudies, Professor, 生命科学研究科, 教授 (70109049)
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| Project Period (FY) |
1998 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥33,200,000 (Direct Cost: ¥33,200,000)
Fiscal Year 2000: ¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 1999: ¥14,200,000 (Direct Cost: ¥14,200,000)
Fiscal Year 1998: ¥14,900,000 (Direct Cost: ¥14,900,000)
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| Keywords | glycopeptide / glycosidase / transglycosidation / glutathione / aminopeptidase / γ-glutamyltranspeptidase / cAMP / pseudohyphal growth / チロシンフェノールリアーゼ / グルコース受容体 / チラミン酸化酵素 / 大腸菌 / ペプチダーゼ / モノアミン酸化酵素 / 出芽酵母 / レセプター / 結晶構造解析 |
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| Research Abstract |
1. We analyzed the function of specific glycosidases produced by microorganisms and attempted to produce useful substances using these enzymes. (a) Enzymatic syntheses of various bioactive glycopeptides were carried out using transglycosylation activity of microbial glycosidases. (b) Effect of glycosylation on the function of protein was investigated using microbial glycosidases.
2. We found that aminopeptidases A, B and N, and dipeptidase D with broad substrate specificity are the four cysteinylglycinases of Escherichia coli K-12. Enzymatic characteristics of purified aminopeptidase B were determined.
3. We identified that the catalytic nucleophile of Escherichia coli γ-glutamyltranspeptidase is the Thrresidue at the N-terminal of the small subunit by a new novel affinity labeling agent.
4. We found that Gpr1, a putative G-protein coupled receptor, regulated glucose dependent cellular cAMP level in yeast Saccharomyces cerevisiae. Functional analysis revealed that pseudohyphal development observed under high glucose and low nitrogen condition was reduced in the GPR1 gene disruptant. We also clarified that the reduced transcriptional level of FLO11 gene which encodes cell surface protein involved in cell adhesion caused pseudohyphal defect in the GPR1 disruptant.
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