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相关概念视频

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

8.9K
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...
8.9K
Enzymes02:34

Enzymes

82.8K
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...
82.8K
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

4.1K
The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
Most enzymes...
4.1K
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

10.8K
The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
10.8K
Enzyme Kinetics01:19

Enzyme Kinetics

99.0K
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
99.0K
Induced-fit Model01:13

Induced-fit Model

82.3K
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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相关实验视频

Updated: Sep 17, 2025

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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在酶催化过程中的模糊性.

Sachin S Katti1, Tvesha Parikh2, Rachel J Godek2

  • 1Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA.

Current opinion in structural biology
|June 28, 2025
PubMed
概括

本质上无序的蛋白质利用动态的动态.

科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 酶学 是一种酶学.

背景情况:

  • 内在无序的蛋白质/区域 (IDPs/IDRs) 对于细胞过程至关重要.
  • 动态电荷:电荷相互作用,称为"模糊"相互作用,是IDP/IDR的特征.
  • 这些相互作用对于酶调节和蛋白激酶和酸酶中的基质招募至关重要.

研究的目的:

  • 审查了解模糊相互作用的最新进展.
  • 阐明分子间和分子内模糊相互作用在酶组合,激活和基质招募中的作用.
  • 突出一种新的蛋白质抑制机制,涉及与活性位点金属的模糊相互作用.

主要方法:

  • 关于内在无序蛋白质和模糊相互作用的最新研究的文献综述.
  • 对专注于蛋白质激酶,酸酶及其调节剂/基质的研究进行分析.
  • 检查酶调节和抑制中的模糊相互作用的具体例子.

主要成果:

  • 模糊相互作用调解酶组合,激活和基质招募用于激酶和酸酶.
  • 分子间和分子内模糊相互作用是这些调节过程的关键.
  • 已经确定了一种独特的抑制机制,涉及蛋白质酸酶和活性位点金属之间的动态模糊相互作用.

更多相关视频

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs

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相关实验视频

Last Updated: Sep 17, 2025

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs

Published on: January 17, 2020

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结论:

  • 模糊的相互作用对于固有无序蛋白质在酶调节中的功能至关重要.
  • 这些相互作用为控制激酶和酸酶活性提供了一种多功能机制.
  • 鉴定到的抑制机制为蛋白质调节和潜在的治疗点提供了新的见解.