对金属酶杂合性不同方面的机理认识。

3区 生物学 Q1 Biochemistry, Genetics and Molecular Biology
Ankita Tripathi, Kshatresh Dutta Dubey
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引用次数: 0

摘要

酶是自然界催化复杂反应的终极机器。虽然酶是为催化特定反应而进化的,但它们在反应和底物选择方面也表现出明显的杂交性。金属酶的活性位点含有金属离子或金属辅助因子,这对其催化活性至关重要。根据金属及其配位环境的不同,金属离子或辅助因子可充当路易斯酸或碱以及氧化还原中心,从而催化大量的自然反应。事实上,金属离子氧化态的多样性使金属酶具有高度的催化适应性和杂交性。在本章中,我们将以最近的几项实验和理论研究为案例,讨论金属酶杂合性的不同方面。我们首先介绍了杂交性的概念,然后深入探讨了分子水平上杂交性的机理。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The mechanistic insights into different aspects of promiscuity in metalloenzymes.

Enzymes are nature's ultimate machinery to catalyze complex reactions. Though enzymes are evolved to catalyze specific reactions, they also show significant promiscuity in reactions and substrate selection. Metalloenzymes contain a metal ion or metal cofactor in their active site, which is crucial in their catalytic activity. Depending on the metal and its coordination environment, the metal ion or cofactor may function as a Lewis acid or base and a redox center and thus can catalyze a plethora of natural reactions. In fact, the versatility in the oxidation state of the metal ions provides metalloenzymes with a high level of catalytic adaptability and promiscuity. In this chapter, we discuss different aspects of promiscuity in metalloenzymes by using several recent experimental and theoretical works as case studies. We start our discussion by introducing the concept of promiscuity and then we delve into the mechanistic insight into promiscuity at the molecular level.

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来源期刊
Advances in protein chemistry and structural biology
Advances in protein chemistry and structural biology BIOCHEMISTRY & MOLECULAR BIOLOGY-
CiteScore
7.40
自引率
0.00%
发文量
66
审稿时长
>12 weeks
期刊介绍: Published continuously since 1944, The Advances in Protein Chemistry and Structural Biology series has been the essential resource for protein chemists. Each volume brings forth new information about protocols and analysis of proteins. Each thematically organized volume is guest edited by leading experts in a broad range of protein-related topics.
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