Regulation of the transition states of the enzymes for alkane production by controlling their conformational fluctuations
Project/Area Number |
15KT0139
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 特設分野 |
Research Field |
Transition State Control
|
Research Institution | The University of Tokyo |
Principal Investigator |
Arai Munehito 東京大学, 大学院総合文化研究科, 教授 (90302801)
|
Co-Investigator(Kenkyū-buntansha) |
林 勇樹 東京大学, 大学院総合文化研究科, 助教 (90444059)
|
Project Period (FY) |
2015-07-10 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
Keywords | タンパク質 / 酵素反応 / 分子動力学 / NMR / バイオエネルギー |
Outline of Final Research Achievements |
Recent advances in protein chemistry have revealed that global conformational change of an enzyme is closely related to formation of the transition state and thus constitutes the rate-determining step in an enzyme reaction. Here, using two enzymes, acyl-ACP reductase (AAR) and aldehyde-deformylating oxygenase (ADO), which are indispensable for biofuel production, we detected conformational fluctuations of enzymes by molecular dynamics simulations (theory) and NMR relaxation measurements (experiment). We then searched for residues essential for controlling conformational fluctuations of the enzymes. Introduction of mutations at these residues resulted in changes of activities, indicating that regulation of the transition state of an enzyme is possible by such mutations. We also performed comprehensive mutational analysis including alanine-scanning mutagenesis on AAR and ADO by making more than 600 mutants and succeeded in identifying the residues important for controlling activities.
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Report
(4 results)
Research Products
(39 results)
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[Journal Article] Interaction of the GntR-family transcription factor Sll1961 with thioredoxin in the cyanobacterium Synechocystis sp. PCC 68032018
Author(s)
Kujirai, J., Nanba, S., Kadowaki, T., Oka, Y., Nishiyama, Y., Hayashi, Y., Arai, M. and Hihara, Y.
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Journal Title
Sci. Rep.
Volume: 8
Issue: 1
Pages: 6666-6666
DOI
Related Report
Peer Reviewed / Open Access
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