Reaction mechanism of novel tryptophan-hydroxylating enzyme involving in quinone cofactor biogenesis
| Project/Area Number |
15K07391
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
中井 忠志 広島工業大学, 生命学部, 准教授 (00333344)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | キノン補酵素 / FAD / オキシゲナーゼ / モノオキシゲナーゼ / X線結晶構造解析 / 分子内架橋 / チオエーテル架橋 / チオエーテル結合 |
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| Outline of Final Research Achievements |
We have studied the reaction mechanism and X-ray crystal structure of FAD-dependent monooxygenase QhpG that is involved in the cofactor biogenesis of bactral quinohemoprotein amine dehydrogenase. Our final aim is application of QhpG for a novel tool for peptide engineering. In vitro reaction system for QhpG provided the important information for the chemical structure of the QhpG reaction product. On the basis of X-ray crystal structure of QhpG, we have elucidated the QhpG reaction mechanism including the recognition of the specific Trp residue on the substrate peptide.
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Report
(4 results)
Research Products
(29 results)
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[Journal Article] Probing the Catalytic Mechanism of Copper Amine Oxidase from Arthrobacter globiformis with Halide Ions.2015
Author(s)
Murakawa, T., Hamaguchi, A., Nakanishi, S., Kataoka, M., Nakai, T., Kawano, Y., Yamaguchi, H., Hayashi, H., Tanizawa, K., and Okajima, T.
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Journal Title
J. Biol. Chem.
Volume: 290
Issue: 38
Pages: 23094-23109
DOI
Related Report
Peer Reviewed
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