Elucidation of novel enzymatic system involved in the activation of the defensive secondary metabolites in the tulip
| Project/Area Number |
23780120
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Bioproduction chemistry/Bioorganic chemistry
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| Research Institution | Toyama Prefectural University |
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Principal Investigator |
NOMURA Taiji 富山県立大学, 工学部, 助教 (40570924)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | チューリップ / チューリッポシド / チューリッパリン / チューリッポシド変換酵素 / カルボキシルエステラーゼ / 二次代謝 / 生合成 / 酵素 |
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| Research Abstract |
This study was performed to identify the enzymes involved in the conversion of tuliposides (Pos), the major secondary metabolites in tulip, to antimicrobial tulipalins (Pa), the lactonized aglycons of Pos. I found that PosA and PosB, which are the major forms of Pos in the tulip cultivar, are converted to the corresponding PaA and PaB by PosA-converting enzyme and PosB-converting enzyme, respectively. Amino acid sequences of those enzymes were similar to the carboxylesterases, which typically catalyze hydrolysis reactions. However, the Pos-converting enzymes catalyzed no hydrolysis of Pos, but the formation of Pa through lactonization. Pos-converting enzymes were identified as the unique lactone-forming carboxylesterases, specifically catalyzing intramolecular transesterification.
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Report
(4 results)
Research Products
(42 results)
