| Project/Area Number |
09672137
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemical pharmacy
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| Research Institution | The University of Tokyo |
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Principal Investigator |
SHIBUYA Masaaki The University of Tokyo, Graduate School of Pharmaceutical Sciences, Assistant Professor, 大学院・薬学系研究科, 助手 (50170923)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 1998: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1997: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | p-coumaroyltriacetic acid synthase / p-coumaroyltriacetic acid lactone / Hydrangea macrophylla var. thunbergii / chalcone systhase / stilbene synthase / 反応機構 / 還元酵素 |
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| Research Abstract |
Chalcone synthase (CHS) and stilbene synthase (STS) are plant-specific polyketide synthases (PKSs). They catalyze common three consecutive decarboxylative condensations and specific cyclization reactions. They are highly homologous to each other, and are likely to fall into a family of PKSs along with acridone synthase and bibenzyl synthase. Two cDNA clones (named as HmC and HmS) both of which show high homology to the known CHSs, were obtained from leaves of Hydrangea macrophylla var. thunbergii. They were expressed in Escherichia coli in order to determine their enzyme functions. Detection of chalcone formation clearly indicated that HmC encoded CHS, while HmS protein catalyzed the formation of neither chalcone nor stilbene. However, a novel pyrone, a lactonization product of a linear tetraketide was detected in reaction products of HmS protein. This proves that HmS encodes a novel PKS which catalyzes only chain elongation without cyclization.
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