Unification of biosynthetic pathways of a variety of plant polyketides
| Project/Area Number |
25242067
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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 |
Biomolecular chemistry
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| Research Institution | University of Shizuoka |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
MORITA HIROYUKI 富山大学, 和漢医薬学総合研究所, 教授 (20416663)
UMEHARA KAORU 静岡県立大学, 薬学部, 講師 (40185070)
WATANABE KENJI 静岡県立大学, 薬学部, 教授 (50360938)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥47,580,000 (Direct Cost: ¥36,600,000、Indirect Cost: ¥10,980,000)
Fiscal Year 2015: ¥8,840,000 (Direct Cost: ¥6,800,000、Indirect Cost: ¥2,040,000)
Fiscal Year 2014: ¥15,730,000 (Direct Cost: ¥12,100,000、Indirect Cost: ¥3,630,000)
Fiscal Year 2013: ¥23,010,000 (Direct Cost: ¥17,700,000、Indirect Cost: ¥5,310,000)
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| Keywords | ポリケタイド / 生合成 / 反応機構 / タンパク質結晶構造解析 / 植物 / 酵素工学 / 閉環酵素 / X線結晶構造解析 / Type III PKS / polyketide synthase / OAC |
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| Outline of Final Research Achievements |
We showed the possibility that tyrosine 72 and histidine 78 was a catalyst residue of OAC from analysis and a variation introduction experiment of the complex X-rays crystal structure with the Oribe Thor acid which was Oribe Thor acid closure enzyme (OAC) derived from hemp and the product. Furthermore, We clarified what enzyme activity attenuated when bulky substituted the amino acid residue which formed a pentyl-binding pocket full of the hydrophobicity that we found in an active site of OAC for a higher bulky residue. Based on the X-ray crystallographic analysis about these variation enzymes, the capacity of the pentyl-binding pocket decreased by introduction of the variation, and a substrate became hard to be connected, it became clear to attenuate enzyme activity.
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Report
(4 results)
Research Products
(30 results)
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[Journal Article] A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin.2015
Author(s)
Noike, M., Matsui, T., Ooya, K., Sasaki, I., Ohtaki, S., Hamano, Y., Maruyama, C., Ishikawa, J., Satoh, Y., Ito, H., Morita, H. and Dairi T.
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Journal Title
Nature Chemical Biology
Volume: 11
Issue: 1
Pages: 71-76
DOI
NAID
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Structural basis for the formation of acylalkylpyrones from two β-ketoacyl units by the fungal type III polyketide synthase CsyB2015
Author(s)
Mori, T., Yang, D., Matsui, T, Hashimoto, M., Morita, H., Fujii, I., Abe, I.
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Journal Title
J. Biol. Chem.
Volume: 290
Issue: 8
Pages: 5214-5225
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Expression, purification, and crystallization of a fungal type III polyketide synthase that produces the csypyrones2014
Author(s)
Yang, D., Mori, T., Matsui, T., Hashimoto, M., Morita, H., Fujii, I., Abe, I.
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Journal Title
Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun.
Volume: 70
Issue: 6
Pages: 730-733
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] Cloning and structure-function analyses of quinolone- and acridone-producing novel type III polyketide synthases from Citrus microcarpa2013
Author(s)
Mori, T., Shimokawa, Y., Matsui, T., Kinjo, K., Kato, R., Noguchi, H., Sugio, S., Morita, H., Abe, I.
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Journal Title
J. Biol. Chem.
Volume: 288
Issue: 40
Pages: 28845-28858
DOI
Related Report
Peer Reviewed
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[Presentation] Natural products from fungi2013
Author(s)
Kenji Watanabe
Organizer
3rd International Conference on Natural product Biosynthesis
Place of Presentation
University of California Los Angeles, University of Southern California (USA)
Related Report
Invited
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