期刊
FEBS LETTERS
卷 587, 期 17, 页码 2772-2777出版社
WILEY
DOI: 10.1016/j.febslet.2013.07.028
关键词
Enzyme kinetics; Thermodynamics; Michaelis-Menten; Reversible reaction
资金
- European Research Council [260392]
- Israel Science Foundation [750/09]
- Helmsley Charitable Foundation
- Larson Charitable Foundation
- Estate of David Arthur Barton
- Anthony Stalbow Charitable Trust
- Stella Gelerman (Canada)
- German Research Foundation [Ll 1676/2-1]
- Azrieli Foundation
- European Research Council (ERC) [260392] Funding Source: European Research Council (ERC)
Michaelis and Menten's mechanism for enzymatic catalysis is remarkable both in its simplicity and its wide applicability. The extension for reversible processes, as done by Haldane, makes it even more relevant as most enzymes catalyze reactions that are reversible in nature and carry in vivo flux in both directions. Here, we decompose the reversible Michaelis-Menten equation into three terms, each with a clear physical meaning: catalytic capacity, substrate saturation and thermodynamic driving force. This decomposition facilitates a better understanding of enzyme kinetics and highlights the relationship between thermodynamics and kinetics, a relationship which is often neglected. We further demonstrate how our separable rate law can be understood from different points of view, shedding light on factors shaping enzyme catalysis. (c) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据