Modifying Hydrolases to Catalyze New Bond Formation Reactions

修饰水解酶以催化新键形成反应

• 批准号: 0616560
• 负责人: Romas Kazlauskas
• 金额: --
• 依托单位: University of Minnesota-Twin Cities
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-08-01 至 2010-01-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=0616560&HistoricalAwards=false
• 关键词: Modifying; Hydrolases; Catalyze; New; Bond

This project will attempt to modify biocatalysts so that they can catalyze industrially relevant reactions. The first objective is to identify and extend the essential catalytic elements in epoxide hydrolases in order for them to accept external nucleophiles. Ability of the epoxide hydrolases to accept external nucleophiles could lead to non-natural but synthetically useful reactions. The second objective is to identify and extend the essential catalytic elements in hydroxynitrile lyase in order for them to accept carbon nucleophiles other than cyanide. This objective could also lead to non-natural but synthetically useful reactions.With this award, the Organic and Macromolecular Chemistry Program is supporting the research of Professor Romas J. Kazlauskas of the Department of Biochemistry at University of Minnesota-Twin Cities. Professor Kazlauskas's research efforts revolve around the modification of biocatalysts to catalyze non-natural but synthetically useful reactions. Such reactions are environmentally friendly, as they reduce costs as well as pollution. These reactions could improve the preparation of fine chemicals, which are needed in chemical and pharmaceutical industries.

该项目将尝试对生物催化剂进行修饰，使其能够催化与工业相关的反应。第一个目标是确定和扩展环氧化物水解酶中的基本催化元件，以便它们能够接受外部亲核试剂。环氧化物水解酶接受外部亲核试剂的能力可能会导致非自然但在合成上有用的反应。第二个目标是确定和扩展羟腈裂解酶中的基本催化元件，以便它们能够接受氰化物以外的碳亲核试剂。这一目标也可能导致非自然但合成有用的反应。凭借这一奖项，有机和高分子化学项目支持明尼苏达大学双子城分校生物化学系的Romas J.Kazlauskas教授的研究。卡兹劳斯卡斯教授的研究工作围绕着对生物催化剂的修饰，以催化非自然但合成有用的反应。这种反应是环保的，因为它们既减少了成本，又减少了污染。这些反应可以改进精细化学品的制备，这是化工和制药行业所需的。