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相关概念视频

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

8.1K
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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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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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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Catalysis02:50

Catalysis

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The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
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Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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Updated: Jun 29, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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使用绑定的辅助因子进行异质生物催化反应的动态模型.

Rowan McDonough1, Charlotte C Williams2, Carol J Hartley3

  • 1Institute for Nanoscale Science and Technology, School of Chemical and Physical Sciences, Flinders University, Bedford Park, SA 5042, Australia.

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PubMed
概括
此摘要是机器生成的。

研究纳米粒子 (SiNPs) 上的酶动力学揭示了合成生物学效率的提高. 结合的尼古丁胺胺氨基二核酸 (NAD+) 提高了酶的性能,这对于增值化学品生产至关重要.

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科学领域:

  • 生物催化剂是一种生物催化剂.
  • 酶动力学 酶动力学
  • 合成生物学 合成生物学

背景情况:

  • 接口酶动力学对于合成生物系统至关重要.
  • 依赖NAD+的酶是生物化学路径中的关键催化剂.

研究的目的:

  • 为了研究NAD+依赖酶的界面动力学.
  • 了解涉及NAD+与纳米粒子 (SiNPs) 连接的催化作用.

主要方法:

  • 采用了两种动力学方法:酶过剩和反应剂 (NAD+) 过剩.
  • 开发了动力模型来描述吸附,复杂化和催化.
  • 在SiNP表面分析了酶和辅因子相互作用.

主要成果:

  • 观察到一种缩效应,导致SiNPs上的高局部酶和NAD+度.
  • 由于表面结合的NAD+导致酶/NAD+复合和催化率的增强.
  • 与自由酶系统相比,在绑定的NAD +系统中实现了更高的酶效率.

结论:

  • 酶吸附到固体基质上与结的催化剂,如NAD+,可以显著提高酶的效率.
  • 这种方法有可能开发高效的流动生物催化系统.
  • 了解界面动力学对于设计先进的合成生物应用至关重要.