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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Understanding Instability in complex enzyme-driven reaction networks
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Understanding Instability in complex enzyme-driven reaction networks

机译：了解复杂的酶驱动反应网络中的不稳定性

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摘要

Much attention has been paid recently to testability and switch-like behavior that might be resident in important biochemical reaction networks. There is, in fact, a great deal of subtlety in the relationship between the structure of a reaction network and its capacity to engender bistability. In common physicochemical settings, large classes of extremely complex networks, taken with mass action kinetics, cannot give rise to bistability no matter what values the rate constants take. On the other hand, bistable behavior can be induced in those same settings by certain very simple and classical mass action mechanisms for enzyme catalysis of a single overall reaction. We present a theorem that distinguishes between those mass action networks that might support bistable behavior and those that cannot. Moreover, we indicate how switch-like behavior results from a well-studied mechanism for the action of human dihydrofolate reductase, an important anti-cancer target.
机译：最近，人们对可测试性和类似开关的行为给予了极大关注，这些行为可能存在于重要的生化反应网络中。实际上，反应网络的结构与其产生双稳态的能力之间的关系有很多微妙之处。在常见的物理化学环境中，无论质量常数如何取值，以质量动力学为基础的大量极其复杂的网络都不会引起双稳态。另一方面，双稳态行为可以通过某些非常简单和经典的质量作用机理在单个相同的反应中进行酶催化而在相同的条件下诱发。我们提出了一个定理，将可能支持双稳态行为的大规模行动网络与不能支持双稳态行为的大规模行动网络区分开。此外，我们指出开关样的行为是如何通过对人类二氢叶酸还原酶（一种重要的抗癌靶标）作用的深入研究而产生的。

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