Molecular Design and Evolution Engineering for Compositc Biochatalysts
复合生物催化剂的分子设计和进化工程
基本信息
- 批准号:13125101
- 负责人:
- 金额:$ 4.16万
- 依托单位:
- 依托单位国家:日本
- 项目类别:Grant-in-Aid for Scientific Research on Priority Areas
- 财政年份:2001
- 资助国家:日本
- 起止时间:2001 至 2003
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
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.
研究了复合生物催化剂的结构和功能,构建了新型复合生物催化剂。Toraya等人基于钴胺依赖二醇脱水酶的三维结构建立了精细的催化机理,并通过理论计算证明了其能量可行性。利用蛋白质工程技术对酶的活性进行了修饰。采用几种脱酶模型构建钴胺素复合催化剂。Tanizawa等人阐明了铜胺氧化酶中含有的由特定酪氨酸残基产生的托喹酮辅因子的生物合成和催化功能的分子机制。此外,在喹诺铁血蛋白胺脱氢酶中发现了一种新的色氨酸衍生的醌辅助因子——半胱氨酸色氨酸醌。Miura等人通过将人工黄素掺入黄酶载脂蛋白中获得了具有新型反应性的黄酶。Horiike等人揭示了外二醇双加氧酶的底物特异性和这些酶的0_2活化的分子基础。Hayashi等人通过对质子转移过程的分析,阐明了吡哆醛酶的精细催化反应机理,从而提出了对“诱导契合”和“多底物识别”的分子理解。Hirotsu等人测定了各种天然复合生物催化剂的三维结构。Esaki等人揭示了铁硫团簇的生物合成机制,并开发了一种利用新型复合生物催化剂生产手性化合物的新工艺。Shimada等人表明,将化学修饰的血红素掺入血红素蛋白中是制备高效蛋白质基催化剂的有力工具。Kitazume等人证明了催化抗体在离子液体中表现出一种新的功能。
项目成果
期刊论文数量(450)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
後藤祐児, 谷澤克行(編著): "バイオサイエンスの新世紀3 タンパク質の分子設計"共立出版株式会社. 201 (2001)
后藤裕二、谷泽胜幸(编):《生物科学的新世纪3:蛋白质的分子设计》共立出版201(2001)
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- 影响因子:0
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Hirofumi Nakajima: "Accurate measurement of near-micromolar oxygen concentrations in aqueous solutions based on enzymatic extradiol cleavage of 4-chlorocatechol : applications to improved low-oxygen experimental systems and quantitative assessment of back
Hirofumi Nakajima:“基于 4-氯儿茶酚的酶促 Extradiol 裂解,精确测量水溶液中近微摩尔氧浓度:在改进的低氧实验系统和定量评估中的应用
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鏡山博行, 三浦 洌, 虎谷哲夫: "補酵素作用のダイナミズム-酵素の機能を支えるアポタンパクの働き-"ビタミン. 76. 273-282 (2002)
Hiroyuki Kagamiyama、Satoshi Miura、Tetsuo Toratani:“辅酶作用的动态 - 支持酶功能的脱辅基蛋白的功能 -”维生素。 76. 273-282 (2002)
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S.Hirota, et al.: "Spectroscopic Observation of Intermediates Formed during the Oxidative Half Reaction of Copper/Topa Quinone-Containing Phenylethylamine Oxidase"Biochemistry. 40. 15789-15796 (2001)
S.Hirota等人:“含铜/托帕醌的苯乙胺氧化酶的氧化半反应过程中形成的中间体的光谱观察”生物化学。
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- 影响因子:0
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Toraya, T., Oka, T., Ando, M., Yamanishi, M., Nishihara, H.: "Novel Pathway for Utilization of Cyclopropanecarboxylate by Rhodococcus rhodochrous."Appl.Environ.Microbiol. 70(1). 224-228 (2004)
Toraya, T.、Oka, T.、Ando, M.、Yamanishi, M.、Nishihara, H.:“红球菌利用环丙烷羧酸盐的新途径。”Appl.Environ.Microbiol。
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TORAYA Tetsuo其他文献
TORAYA Tetsuo的其他文献
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{{ truncateString('TORAYA Tetsuo', 18)}}的其他基金
Studies of action mechanisms of radical enzyme systems for providing new paradigms of enzyme researches
自由基酶系统作用机制研究为酶研究提供新范式
- 批准号:
22570143 - 财政年份:2010
- 资助金额:
$ 4.16万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Structural biochemistry of radical-utilizing enzymes and their activating proteins
自由基利用酶及其激活蛋白的结构生物化学
- 批准号:
17370038 - 财政年份:2005
- 资助金额:
$ 4.16万 - 项目类别:
Grant-in-Aid for Scientific Research (B)
Mechanisms of Radical Catalysis in Vitamin B_<12> Enzyme and Reactivation by Molecular Chaperone-like Factor
维生素B_<12>酶的自由基催化机制及类分子伴侣因子的再激活
- 批准号:
13480195 - 财政年份:2001
- 资助金额:
$ 4.16万 - 项目类别:
Grant-in-Aid for Scientific Research (B)
Studies on the Structure and the Mechanism of Radical Enzymes
自由基酶的结构与作用机制研究
- 批准号:
10680611 - 财政年份:1998
- 资助金额:
$ 4.16万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
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