Bronsted Analysis of Catalytic Promicuity in Enzyme Models and Model Enzymes

酶模型和模型酶中催化相似性的布朗斯台德分析

• 批准号: EP/E019390/1
• 负责人: Florian Hollfelder
• 金额: $ 37.48万
• 依托单位: University of Cambridge
• 依托单位国家: 英国
• 项目类别: Research Grant
• 财政年份: 2007
• 资助国家: 英国
• 起止时间: 2007 至 无数据
• 项目状态: 已结题
• 来源: https://gtr.ukri.org/projects?ref=EP%2FE019390%2F1
• 关键词: Bronsted; Analysis; Catalytic; Promicuity; Enzyme

Most biological processes involve the action of enzymes, which are central for explaining the workings of living cells and organisms. However, there is no comprehensive quantitative understanding of enzyme action and our current understanding certainly fails the most severe test, that of producing catalysts with rates that rival natural enzymes. Catalysis is defined as transition state stabilisation. We will apply a tool from physical-organic chemistry, linear-free energy relationships, to characterise these transitions states in catalytic systems that have not just one, but several activities (a phenomenon called 'catalytic promiscuity'). We hope to gain detailed insight into the bond-making and -breaking processes in these remarkable catalysts, to trace the evolution of a catalytic machinery on the basic level of mechanistic chemistry and learn about the nature of their transition states.

大多数生物过程都涉及酶的作用，酶是解释活细胞和生物体运作的核心。然而，对酶的作用还没有全面的定量理解，我们目前的理解肯定无法通过最严格的测试，即生产出与天然酶相媲美的催化剂。催化作用被定义为过渡态稳定。我们将应用物理有机化学的工具，线性自由能量关系，来描述催化系统中的这些过渡状态，这些过渡状态不仅有一个，而且有几个活动（一种称为“催化滥交”的现象）。我们希望深入了解这些卓越催化剂的成键和断键过程，在机械化学的基础上追踪催化机制的演变，并了解其过渡态的本质。

项目成果

Transition-State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase.

混杂酶中的过渡态相互作用：铜绿假单胞菌芳基硫酸酯酶水解硫酸盐和磷酸单酯。

• DOI: 10.1021/acs.biochem.8b00996
• 发表时间: 2019
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Van Loo B