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相关概念视频

Induced-fit Model01:13

Induced-fit Model

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Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
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Enzymes02:34

Enzymes

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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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Allosteric Proteins-ATCase01:19

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Introduction to Mechanisms of Enzyme Catalysis01:13

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Introduction to Mechanisms of Enzyme Catalysis01:13

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Updated: Apr 1, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
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由不同形态路径赋予的酶基质特异性

Florencia Rago1, Daniel Saltzberg2, Karen N Allen1,3

  • 1Program in Biochemistry and Molecular Biology (BMB), Boston University , Boston, Massachusetts 02215, United States.

Journal of the American Chemical Society
|October 7, 2015
PubMed
概括
此摘要是机器生成的。

酶形状的变化决定了基质的特异性. 阿尔多酶使用不同的构造来区分果糖1-酸和果糖1,6-二酸,将构造变化与催化联系起来.

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科学领域:

  • 生物化学
  • 酶动力学
  • 蛋白质的结构动态

背景情况:

  • 酶催化依赖基质识别,但直接证据将酶形状变化与基质选择性联系在一起是有限的.
  • 一个关键的糖解酶阿尔多酶必须区分果糖1-酸和果糖1,6-二酸,使其成为研究基质区分的理想模型.
  • 已知远离活性部位的异酶特异残留物 (ISRs),特别是表面α螺旋和基终端区域 (CTR),可以调解运动区别.

研究的目的:

  • 调查酶构成变化是阿尔多酶基质选择性的假设.
  • 探索特定区域的作用,包括表面α螺旋和CTR,调解这些形状变化.
  • 确定观察到的形状动态与催化过程之间的联系.

主要方法:

  • 创建单个表面氨酸变体用于特定地点的标签.
  • 用对环境敏感的光剂标记变种.
  • 使用光辐射光谱法和停止流量的光光谱法监测构造变化.

主要成果:

  • 标记的阿尔多酶变体的光谱在和量中的果糖1-酸盐与果糖1,6-二酸盐存在差异,表明不同的构造.
  • 在光光谱中依赖基质度的变化证实了结合事件.
  • 停止流动的光测量显示,形状变化的速率与催化发生在相同的时间范围内.

结论:

  • 阿尔多酶表现出基质特异性的形状变化.
  • 这些形态动态与酶的催化循环和基质识别有关.
  • 在具有多个基质的酶中,形状变化代表了基质特异性的潜在常见机制.