Multidimensional energy analysis of pyridoxal-enzyme and quinoenzyme reactions
Project/Area Number |
21570120
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Osaka Medical College |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
TAKESHI Murakawa 大阪医科大学, 医学部, 助教 (90445990)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2009: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | プロトン移動 / ピリドキサール酵素 / キノン酵素 / 反応機構 / エネルギー準位 / セリンパルミトイル転移酵素 / トレオニン合成酵素 / 銅アミン酸化酵素 / 立体化学 / 酵素反応機構 / 遷移相速度論 / X線結晶解析 / ピリドキサールリン酸 / タンパク質のゆらぎ / 計算化学 / エネルギー進位 |
Research Abstract |
Multidimensional free energy analysis of the reactions of the catalytic reactions of two pyridoxal enzymes(serine palmitoyltransferase and threonine synthase) and a quinoenzyme cupper amine oxidase were carried out to elucidate the energetic mechanism of these enzymes. The mechanisms by which the versatile catalyst pyridoxal phosphate is organized to catalyze only one type of reaction, i. e., a stereochemical mechanism and the product-assisted catalysis, were clarified. Analysis of the reaction of cupper amine oxidase, together with the ultra-high-resolution structure of the enzyme, revealed that the dynamic motion of the enzyme provides the basis for the quantum tunneling effect that promotes its catalysis.
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Report
(4 results)
Research Products
(22 results)
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[Journal Article] Role of a conserved arginine residue during catalysis in serine palmitoyltransferase2011
Author(s)
Lowther, J., Charmier, G., Raman, M. C., Ikushiro, H., Hayashi, H., Campopiano, D. J.
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Journal Title
FEBS Lett
Volume: 585
Pages: 1729-1734
Related Report
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[Journal Article] Analysis of mammalian histidine decarboxylase dimerization interface reveals an electrostatic hotspot important for catalytic site topology and function2011
Author(s)
Moya-Garcia, A. A., Rodriguez-Agudo, D., Hayashi, H., Medina, M. A., Urdiales, J. L., Sanchez-Jimenez, F.
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Journal Title
J. Chem. Theory. Comput
Volume: 7
Pages: 1935-1942
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[Journal Article] Structural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorum2009
Author(s)
Ikushiro, H., Islam, M. M., Okamoto, A., Hoseki, J., Murakawa, T., Fujii, S., Miyahara, I., Hayashi, H.
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Journal Title
J Biochem
Volume: 146
Pages: 549-562
NAID
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