active site

简明释义

活性中心

英英释义

例句

1.The specificity of an enzyme is largely due to the unique shape of its active site.

酶的特异性主要是由于其活性位点的独特形状。

2.Inhibitors can bind to the active site, preventing the enzyme from catalyzing reactions.

抑制剂可以结合到活性位点，阻止酶催化反应。

3.When a substrate binds to the active site, it forms an enzyme-substrate complex.

当底物结合到活性位点时，它形成了酶-底物复合物。

4.Mutations in the gene can alter the structure of the active site and affect enzyme activity.

基因中的突变可以改变活性位点的结构，并影响酶活性。

5.The enzyme's function is determined by the shape of its active site.

酶的功能由其活性位点的形状决定。

作文

The concept of an active site is crucial in the field of biochemistry, particularly when discussing enzymes and their functions. Enzymes are biological catalysts that accelerate chemical reactions in living organisms. Each enzyme has a specific region known as the active site, which is designed to bind to a particular substrate. This binding is essential for the enzyme to perform its catalytic role effectively.To understand the significance of the active site, one must first appreciate how enzymes work. Enzymes lower the activation energy required for a reaction to occur, making it easier for substrates to convert into products. The active site plays a pivotal role in this process by providing a unique environment that facilitates the transformation of substrates. The specificity of the active site ensures that only certain substrates can bind, which is often described by the 'lock and key' model or the 'induced fit' model. In the lock and key model, the substrate fits perfectly into the active site like a key in a lock. In contrast, the induced fit model suggests that the active site undergoes a conformational change upon substrate binding, enhancing the interaction between the enzyme and the substrate.Moreover, various factors can influence the activity of the active site. Temperature, pH, and the concentration of substrates or inhibitors can all affect how well an enzyme performs its function. For instance, if the temperature is too high, it may lead to denaturation of the enzyme, altering the shape of the active site and preventing substrate binding. Similarly, extreme pH levels can disrupt the ionic and hydrogen bonds that maintain the structure of the active site, resulting in decreased enzyme activity.In addition to these factors, the presence of inhibitors can also impact the functionality of the active site. Inhibitors are molecules that can bind to the enzyme and reduce its activity. They can be classified into competitive and non-competitive inhibitors. Competitive inhibitors resemble the substrate and compete for binding at the active site, while non-competitive inhibitors bind to a different part of the enzyme, altering its shape and affecting the active site's ability to catalyze the reaction.Understanding the active site is not only important for biochemistry but also has practical applications in medicine and drug design. Many drugs are designed to target specific enzymes by interacting with their active sites. For example, certain medications used to treat high blood pressure work by inhibiting specific enzymes involved in the regulation of blood vessel constriction. By understanding the structure and function of the active site, scientists can develop more effective drugs with fewer side effects.In conclusion, the active site is a fundamental concept in enzymology that underpins the functioning of enzymes. Its specificity and the factors affecting its activity are vital for understanding biochemical reactions. As research continues to advance in this area, the knowledge surrounding the active site will undoubtedly contribute to significant breakthroughs in fields such as medicine, biotechnology, and beyond.

“活性位点”这一概念在生物化学领域至关重要，尤其是在讨论酶及其功能时。酶是生物催化剂，加速生物体内的化学反应。每种酶都有一个特定区域，称为活性位点，它设计用于与特定底物结合。这种结合对于酶有效地执行其催化作用至关重要。要理解活性位点的重要性，首先必须了解酶的工作原理。酶降低了反应所需的活化能，使底物更容易转化为产物。活性位点在此过程中起着关键作用，它提供了一个独特的环境，促进底物的转化。活性位点的特异性确保只有某些底物能够结合，这通常用“锁和钥匙”模型或“诱导适应”模型来描述。在锁和钥匙模型中，底物完美地适合活性位点，就像钥匙插入锁中一样。相反，诱导适应模型则表明，底物结合后，活性位点会发生构象变化，从而增强酶与底物之间的相互作用。此外，各种因素可以影响活性位点的活性。温度、pH值以及底物或抑制剂的浓度都可能影响酶的功能。例如，如果温度过高，可能导致酶变性，改变活性位点的形状，从而阻止底物结合。同样，极端的pH值也会破坏维持活性位点结构的离子键和氢键，导致酶活性降低。除了这些因素外，抑制剂的存在也会影响活性位点的功能。抑制剂是可以与酶结合并降低其活性的分子。它们可以分为竞争性抑制剂和非竞争性抑制剂。竞争性抑制剂类似于底物，并与活性位点竞争结合，而非竞争性抑制剂则结合在酶的不同部分，改变其形状，从而影响活性位点催化反应的能力。理解活性位点不仅对于生物化学很重要，还在医学和药物设计中具有实际应用。许多药物的设计旨在通过与其活性位点相互作用来靶向特定酶。例如，用于治疗高血压的某些药物通过抑制参与血管收缩调节的特定酶来发挥作用。通过了解活性位点的结构和功能，科学家可以开发出更有效且副作用更少的药物。总之，活性位点是酶学中的基本概念，支撑着酶的功能。它的特异性及影响其活性的因素对于理解生化反应至关重要。随着这一领域研究的不断进展，围绕活性位点的知识无疑将为医学、生物技术等领域的重要突破做出贡献。