Optimization of collective enzyme activity via spatial localization
Optimization of collective enzyme activity via spatial localization
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DOI：
10.1063/1.4823504
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发表时间：
2013-10-07
影响因子：
4.4
通讯作者：
Gerland, Ulrich
中科院分区：
文献类型：
--
作者：
Buchner, Alexander;Tostevin, Filipe;Gerland, Ulrich
酶的空间组织往往在酶的功能和效率中起着至关重要的作用。因此，为了充分了解酶途径的设计和运作，了解酶的相对排列如何影响途径功能是至关重要的。在这里，我们研究了酶定位对反应-扩散模型中最小双酶途径通量的影响。我们考虑了中间底物分子的不同反应动力学、空间维度和损失机制。我们对这一模型的不同制度的系统分析揭示了这些不同制度的现象学中的普遍特征和独特特征。特别是，使反应通量最大化的第二途径酶的分布经历了从第二途径酶催化效率低时与第一途径酶共定位到催化效率高时扩展轮廓的一般转变。然而，关键过渡点和扩展最优剖面的形状受模型特定特征的显著影响。我们用单个底物分子的随机反应和扩散过程来解释这些不同系统的行为。(C) 2013 AIP出版有限责任公司
The spatial organization of enzymes often plays a crucial role in the functionality and efficiency of enzymatic pathways. To fully understand the design and operation of enzymatic pathways, it is therefore crucial to understand how the relative arrangement of enzymes affects pathway function. Here we investigate the effect of enzyme localization on the flux of a minimal two-enzyme pathway within a reaction-diffusion model. We consider different reaction kinetics, spatial dimensions, and loss mechanisms for intermediate substrate molecules. Our systematic analysis of the different regimes of this model reveals both universal features and distinct characteristics in the phenomenology of these different systems. In particular, the distribution of the second pathway enzyme that maximizes the reaction flux undergoes a generic transition from co-localization with the first enzyme when the catalytic efficiency of the second enzyme is low, to an extended profile when the catalytic efficiency is high. However, the critical transition point and the shape of the extended optimal profile is significantly affected by specific features of the model. We explain the behavior of these different systems in terms of the underlying stochastic reaction and diffusion processes of single substrate molecules. (C) 2013 AIP Publishing LLC.