allosteric effect

简明释义

变构效应

英英释义

例句

1.Inhibitors can exert an allosteric effect 变构效应 that alters the shape of the enzyme, reducing its activity.

抑制剂可以施加一个变构效应 变构效应，改变酶的形状，降低其活性。

2.Understanding the allosteric effect 变构效应 is crucial for developing new therapeutic strategies.

理解变构效应 变构效应对于开发新的治疗策略至关重要。

3.Researchers are studying how the allosteric effect 变构效应 influences drug design.

研究人员正在研究变构效应 变构效应如何影响药物设计。

4.The allosteric effect 变构效应 can lead to cooperative binding in multi-subunit proteins.

在多亚基蛋白中，变构效应 变构效应可以导致协同结合。

5.The binding of the first substrate can induce an allosteric effect 变构效应, enhancing the enzyme's activity.

第一个底物的结合可以诱导一个变构效应 变构效应，增强酶的活性。

作文

The concept of the allosteric effect plays a crucial role in biochemistry, particularly in the regulation of enzyme activity. Enzymes are biological catalysts that speed up chemical reactions in living organisms. However, their activity is not solely determined by the concentration of substrates; rather, it can be modulated by various factors, including the presence of other molecules. The allosteric effect refers to the regulation of an enzyme's activity through the binding of an effector molecule at a site other than the active site. This mechanism allows for a more sophisticated level of control over metabolic pathways.When an effector molecule binds to the allosteric site of an enzyme, it induces a conformational change in the enzyme's structure. This change can either enhance or inhibit the enzyme's activity. For instance, in the case of positive allosteric effect, the binding of an activator molecule increases the enzyme's affinity for its substrate, thereby enhancing the reaction rate. Conversely, in the case of negative allosteric effect, the binding of an inhibitor reduces the enzyme's activity, which can prevent the excessive production of certain metabolites.One of the most well-known examples of the allosteric effect is found in the enzyme aspartate transcarbamoylase (ATCase), which plays a key role in the biosynthesis of pyrimidines. ATCase exhibits a classic sigmoidal curve in its reaction kinetics, indicating that its activity is not simply a linear function of substrate concentration. Instead, the enzyme's activity is influenced by the binding of ATP and CTP, which serve as allosteric activators and inhibitors, respectively. The intricate balance between these effectors illustrates how the allosteric effect allows cells to finely tune their metabolic processes in response to changing environmental conditions.The significance of the allosteric effect extends beyond basic biochemistry; it has important implications in drug design and therapeutic interventions. Many modern drugs are designed to target allosteric sites on enzymes rather than active sites, which can lead to more selective and effective treatments with fewer side effects. By understanding the allosteric effect, researchers can develop novel compounds that modulate enzyme activity in a desired manner, offering new avenues for treating diseases such as cancer, diabetes, and neurodegenerative disorders.In conclusion, the allosteric effect is a fundamental concept in the field of biochemistry that highlights the complexity of enzyme regulation. By allowing for the modulation of enzyme activity through the binding of effector molecules, the allosteric effect provides a dynamic mechanism for controlling metabolic pathways. Its importance in both biological systems and pharmacology underscores the need for continued research into this fascinating area of study, as it holds the potential for significant advancements in our understanding of cellular functions and the development of targeted therapies. Understanding the allosteric effect will ultimately enhance our ability to manipulate biological processes for therapeutic benefit, making it a vital topic in modern scientific research.

“变构效应”（allosteric effect）的概念在生物化学中起着至关重要的作用，特别是在酶活性的调节方面。酶是生物催化剂，可以加速生物体内的化学反应。然而，它们的活性并不仅仅由底物浓度决定；相反，它可以通过多种因素进行调节，包括其他分子的存在。“变构效应”指的是通过在活性位点以外的部位结合效应分子来调节酶的活性。这一机制使得对代谢途径的控制更加复杂。当效应分子与酶的变构位点结合时，会引发酶结构的构象变化。这种变化可以增强或抑制酶的活性。例如，在正向变构效应的情况下，激活分子的结合增加了酶对底物的亲和力，从而提高反应速率。相反，在负向变构效应的情况下，抑制剂的结合降低了酶的活性，这可以防止某些代谢产物的过量产生。最著名的变构效应例子之一是天冬氨酸转氨酶（ATCase），它在嘧啶生物合成中发挥关键作用。ATCase在其反应动力学中表现出经典的S型曲线，表明其活性并不是简单的底物浓度的线性函数。相反，酶的活性受到ATP和CTP的结合影响，这些分子分别作为变构激活剂和抑制剂。这些效应器之间的微妙平衡说明了变构效应如何使细胞能够根据不断变化的环境条件精细调节其代谢过程。变构效应的重要性不仅限于基础生物化学；它在药物设计和治疗干预方面也具有重要意义。许多现代药物旨在靶向酶的变构位点，而不是活性位点，这可以导致更具选择性和有效性的治疗，并减少副作用。通过理解变构效应，研究人员可以开发新化合物，以期望的方式调节酶活性，为治疗癌症、糖尿病和神经退行性疾病等疾病提供新的途径。总之，变构效应（allosteric effect）是生物化学领域的一个基本概念，突显了酶调节的复杂性。通过允许通过效应分子的结合来调节酶活性，变构效应提供了一种动态机制，用于控制代谢途径。它在生物系统和药理学中的重要性强调了继续研究这一迷人领域的必要性，因为它具有显著推动我们对细胞功能理解和靶向治疗发展的潜力。理解变构效应最终将增强我们操纵生物过程以获得治疗益处的能力，使其成为现代科学研究中的一个重要主题。