allosteric enzyme

简明释义

变构酶

英英释义

例句

1.Inhibitors can bind to an allosteric enzyme 别构酶, altering its activity without directly blocking the active site.

抑制剂可以结合到一个别构酶 allosteric enzyme上，改变其活性而不直接阻塞活性位点。

2.The regulation of metabolic pathways often involves an allosteric enzyme 别构酶 that can change its shape in response to different molecules.

代谢途径的调节通常涉及到一种别构酶 allosteric enzyme，它可以根据不同的分子改变其形状。

3.Many metabolic disorders are linked to dysfunctional allosteric enzymes 别构酶, which can disrupt normal biochemical pathways.

许多代谢紊乱与功能失常的别构酶 allosteric enzymes有关，这可能干扰正常的生化途径。

4.Understanding how allosteric enzymes 别构酶 work is crucial for drug design and developing new therapies.

理解别构酶 allosteric enzymes 的工作原理对药物设计和开发新疗法至关重要。

5.The feedback inhibition mechanism often involves an allosteric enzyme 别构酶 that helps maintain homeostasis in cells.

反馈抑制机制通常涉及一种别构酶 allosteric enzyme，它有助于维持细胞的稳态。

作文

All living organisms rely on a complex network of biochemical processes to sustain life. One critical component of these processes is enzymes, which act as catalysts to accelerate chemical reactions within cells. Among the various types of enzymes, the concept of the allosteric enzyme (变构酶) stands out due to its unique regulatory mechanisms that play a vital role in metabolic pathways. Understanding allosteric enzymes is essential for grasping how cellular functions are finely tuned and regulated.Allosteric enzymes differ from traditional enzymes in that they can exist in multiple conformational states. This means that their activity can be altered not just by the concentration of substrates but also by the binding of regulatory molecules at sites distinct from the active site. These regulatory sites are known as allosteric sites. When a molecule binds to an allosteric site, it induces a conformational change in the enzyme, which can either enhance or inhibit its activity. This mechanism allows for a more dynamic response to changes in cellular conditions compared to non-allosteric enzymes.One of the key features of allosteric enzymes is their sigmoidal (S-shaped) kinetic curve, which contrasts with the hyperbolic curve typically observed in Michaelis-Menten kinetics of non-allosteric enzymes. The sigmoidal shape indicates that the enzyme's activity is cooperative; as more substrate molecules bind, the enzyme becomes increasingly active. This cooperativity is crucial for regulating metabolic pathways, as it allows for a more sensitive response to fluctuations in substrate levels.A classic example of an allosteric enzyme is phosphofructokinase (PFK), which plays a pivotal role in glycolysis, the pathway that breaks down glucose to produce energy. PFK is regulated by several metabolites, including ATP and AMP. When ATP levels are high, it binds to the allosteric site of PFK, inhibiting its activity and slowing down glycolysis. Conversely, when AMP levels rise, indicating low energy availability, AMP binds to the allosteric site, activating PFK and promoting glycolysis. This intricate regulation ensures that the cell maintains energy homeostasis, adapting to varying energy demands.The study of allosteric enzymes has significant implications in drug design and biotechnology. Many pharmaceutical agents target allosteric sites to modulate enzyme activity, offering a way to influence metabolic pathways without directly competing with substrates. This approach can result in fewer side effects and improved therapeutic outcomes. In biotechnology, understanding allosteric enzymes can lead to the development of engineered enzymes with desired properties for industrial applications, such as biofuels or pharmaceuticals.In conclusion, allosteric enzymes are a fascinating area of study within biochemistry, highlighting the complexity of enzyme regulation and its importance in maintaining cellular function. Their ability to respond dynamically to changes in the cellular environment makes them essential for metabolic control. As research continues to uncover the intricacies of these enzymes, we gain deeper insights into the fundamental processes that sustain life and the potential for innovative applications in medicine and industry.

所有生物体依赖复杂的生化过程网络来维持生命。这些过程中的一个关键组成部分是酶，它作为催化剂加速细胞内的化学反应。在各种类型的酶中，变构酶（allosteric enzyme）的概念因其独特的调节机制而脱颖而出，这在代谢途径中发挥着至关重要的作用。理解变构酶对于掌握细胞功能如何被精细调节至关重要。变构酶与传统酶不同，因为它们可以存在于多种构象状态。这意味着它们的活性不仅可以通过底物浓度改变，还可以通过调节分子在不同于活性位点的结合位点的结合来改变。这些调节位点被称为变构位点。当分子结合到变构位点时，它会诱导酶的构象变化，这可以增强或抑制其活性。这种机制使得相较于非变构酶，细胞条件变化时能够更动态地响应。变构酶的一个关键特征是它们的S形（sigmoidal）动力学曲线，这与非变构酶的米氏动力学通常观察到的双曲线曲线形成对比。S形曲线表明，酶的活性是协同的；随着更多底物分子的结合，酶的活性逐渐增强。这种协同效应对于调节代谢途径至关重要，因为它允许对底物水平波动做出更灵敏的响应。一个经典的变构酶例子是磷酸果糖激酶（PFK），它在糖酵解过程中发挥着关键作用，该过程分解葡萄糖以产生能量。PFK受到几种代谢物的调节，包括ATP和AMP。当ATP水平高时，它结合到PFK的变构位点，抑制其活性并减缓糖酵解。相反，当AMP水平上升时，表示能量可用性低，AMP结合到变构位点，激活PFK并促进糖酵解。这种复杂的调节确保细胞维持能量稳态，适应不同的能量需求。对变构酶的研究在药物设计和生物技术中具有重要意义。许多药物靶向变构位点以调节酶活性，提供了一种影响代谢途径的方法，而不直接与底物竞争。这种方法可能导致更少的副作用和改善的治疗结果。在生物技术中，理解变构酶可以导致开发具有所需特性的工程酶，用于工业应用，如生物燃料或药物。总之，变构酶是生物化学中一个引人入胜的研究领域，突显了酶调节的复杂性及其在维持细胞功能中的重要性。它们能够动态响应细胞环境中的变化，使其成为代谢控制的核心。随着研究不断揭示这些酶的复杂性，我们对维持生命的基本过程以及在医学和工业中创新应用的潜力有了更深入的了解。