Novel pyrethroid-metabolizing enzyme in the silkmoth
Project/Area Number |
21780049
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Single-year Grants |
Research Field |
Applied entomology
|
Research Institution | Kyushu University |
Principal Investigator |
KOHJI Yamamoto 九州大学, 大学院・農学研究院, 助教 (00346834)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2011: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2010: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
|
Keywords | 環境 / 解毒酵素 / 昆虫 / マイクロアレイ / 農薬 / 応用昆虫 / 分子生物学 |
Research Abstract |
Glutathione transferases comprise a major family of detoxification enzyme. Here, we report the substrate specificity, the crystal structure of unclassified GST of Bombyx mori, bmGSTU, and showing that it occurred as a dimer, like other GSTs. The bmGSTU was able to conjugate glutathione to 1-chloro-2, 4-dinitrobenzene, the universal substrate of GST. The structure of bmGSTU was determined with resolutions of 2. 1 A, by synchrotron radiation and molecular replacement method. Each subunit of bmGSTU displayed a glutathione-binding site in the active center. Furthermore, the bmGSTU mRNA was highly expressed in insecticide-resistance strain of B. mori.
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Report
(4 results)
Research Products
(27 results)