Mechanisms of Enzymatic Catalysis

酶催化机制

• 批准号: 9221119
• 负责人: Harvey Fisher
• 金额: $ 24万
• 依托单位: University of Kansas Medical Center
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-02-01 至 1996-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9221119&HistoricalAwards=false
• 关键词: Mechanisms; Enzymatic; Catalysis

The proposed research involves the catalytic mechanism of bovine liver glutamate dehydrogenase. The timing of bond-making and bond- breaking processes as well as proton transfers will be determined for both the forward and reverse reactions catalyzed by the enzyme. The catalytic reaction coordinate will be correlated with enzyme conformation changes which are known to alter solvent access to the active site. Mechanistic results will be correlated with available protein three dimensional structural information to arrive at a unified description of the catalytic process as a function of time. %%% Enzyme mechanism studies characterize the step by step processes involving the enzyme, solvent, and substrate(s) which occur during catalysis. Developing a self-consistent picture of an enzyme mechanism is difficult and laborious, requiring application of structural, chemical, as well as kinetic information. It is the most difficult and potentially most rewarding study that can be undertaken with enzymes, which are in their very essence active and time-dependent entities. Knowledge of mechanism allows manipulation of the enzyme's catalytic machinery to carry out chemistry and permits design of inhibitors of the enzyme which often turn out to be potent drugs.

该研究涉及牛磺酸的催化机理， 肝谷氨酸脱氢酶 债券发行和债券发行的时机- 断裂过程以及质子转移将被确定 用于酶催化的正向和反向反应。 催化反应坐标与酶有关 已知的构象变化会改变溶剂进入 活性部位 机制结果将与可用的 蛋白质的三维结构信息， 作为时间函数的催化过程的统一描述。 %%% 酶机制研究表征了分步过程 涉及酶、溶剂和底物， 催化作用 开发一种酶的自洽图像 机制是困难和费力的，需要应用 结构、化学以及动力学信息。 是 最困难也可能是最有价值的研究 这些酶在本质上是活性的， 时间依赖的实体。 对机制的了解使 操纵酶的催化机制， 化学，并允许设计酶的抑制剂， 往往是强效药物。