| Project/Area Number |
13125101
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Science and Engineering
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
TORAYA Tetsuo Okayama Univ., Faculty of Engineering, Professor, 化学研究所, 教授 (50135597)
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| Co-Investigator(Kenkyū-buntansha) |
HAYASHI Hideyuki Osaka Medical College, Faculty of Medicine, Assoc. Prof., 医学部, 助教授 (00183913)
HAYASHI Katsuyuki Osaka Univ., Institute of Scientific and Industrial Research, Professor, 産業科学研究所, 教授 (20133134)
TORAYA Tetsuo Okayama Univ., Faculty of Engineering, Professor, 工学部, 教授 (70026318)
SHIMADA Hideo Keio Univ., School of Medicine, Assoc. Prof., 医学部, 助教授 (80095611)
HIROTSU Ken Osaka City Univ., Graduate School of Science, Professor, 大学院・理学研究科, 教授 (10047269)
堀池 喜八郎 滋賀医科大学, 医学部, 教授 (80089870)
三浦 洌 熊本大学, 医学部, 教授 (70093466)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥6,500,000 (Direct Cost: ¥6,500,000)
Fiscal Year 2003: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 2002: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 2001: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | composite biocatalyst / coenzyme / structure activity relationship / pyridoxal phosphate / cobalamin / flavin / heme / built-in cofactor / キノヘムプロテイン |
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| Research Abstract |
Structures and functions of composite biocatalysts were studied, and novel composite biocatalysts were constructed. Toraya et al. established a refined catalytic mechanism for cobalamin-dependent diol dehydratase based on its three-dimensional structure and demonstrated its energetic feasibility by theoretical calculations. Reactivity of the enzyme was modified by protein engineering techniques. Cobalamin composite catalysts were constructed using several apoenzyme models. Tanizawa et al. elucidated the molecular mechanism of biosynthesis and catalytic function of the topaquinone cofactor that is contained in copper amine oxidase and produced from a specific tyrosine residue. Furthermore, a new tryptophan-derived quinone cofactor, cysteine tryptophylquinone, in quinohemoprotein amine dehydrogenase was identified. Miura et al. obtained flavoenzymes with novel reactivity by incorporating artificial flavins to flavoenzyme apoproteins. Horiike et al. revealed molecular bases for substrate specificity of extradiol dioxygenases and 0_2 activation by these enzymes. Hayashi et al. elucidated the refined catalytic reaction mechanisms of pyridoxal enzymes by analyzing the proton-transfer process, thereby presenting the molecular understanding of the "induced fit" and "multisubstrate recognition". Hirotsu et al. determined three-dimensional structures of various natural composite biocatalysts. Esaki et al. revealed the mechanism of biosynthesis of iron-sulfur clusters and developed a novel process for the production of chiral compounds by the use of novel composite biocatalysts. Shimada et al. showed that incorporation of a chemically modified heme into heme proteins is a powerful tool for the preparation of a highly efficient protein-based catalyst. Kitazume et al. demonstrated that catalytic antibodies exhibit a novel function in ionic liquids.
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