Engineering of plant-specific polyketide scaffold synthetic enzymes to produce structural diversity of compounds
| Project/Area Number |
26282210
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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 |
Biomolecular chemistry
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| Research Institution | University of Toyama |
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Principal Investigator |
Morita Hiroyuki 富山大学, 和漢医薬学総合研究所, 教授 (20416663)
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| Co-Investigator(Renkei-kenkyūsha) |
MATSUI Takashi 富山大学, 和漢医薬学総合研究所, 助教 (30463582)
KODAMA Takeshi 富山大学, 和漢医薬学総合研究所, 特命助教 (40710207)
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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 |
¥17,030,000 (Direct Cost: ¥13,100,000、Indirect Cost: ¥3,930,000)
Fiscal Year 2016: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
Fiscal Year 2015: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2014: ¥8,710,000 (Direct Cost: ¥6,700,000、Indirect Cost: ¥2,010,000)
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| Keywords | ポリケタイド / 酵素工学 / X線結晶構造解析 / 閉環酵素 / 立体構造解析 / アルカロイド |
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| Outline of Final Research Achievements |
In order to produce structural diversity of compounds, combinatorial biosyntheses of the polyketide cyclase, olivetolic acid cyclase (OAC) and the type III polyketide synthase, octaketide synthase from Aloe arborescens using structurally distinct various CoA thioesters as the substrates were carried out. As a result, we found that the co-incubation of the enzymes using hexanoyl-CoA and malonyl-CoA as the substrates led to a production of novel naphthalene. Furthermore, we solved OAC apo and OAC-olivetolic acid binary complex structures at 1.4 angstrom and 1.7 angstrom resolutions, respectively. The crystallographic and site-directed mutagenesis studies of OAC revealed that the enzyme possesses the pentyl-binding pocket that plays an important role to bind the pentyl moiety of the substrate and employs Tyr72 and His78 as the catalytic residues.
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Report
(4 results)
Research Products
(49 results)
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[Journal Article] Structural insight into the enzymatic formation of bacterial stilbene2016
Author(s)
Mori, T., Awakawa, T., Shimomura, K., Saito, Y., Yang, D., Morita, H., Abe, I.
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Journal Title
Cell Chem. Biol.
Volume: 23
Issue: 12
Pages: 1468-1479
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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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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