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相关概念视频

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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...
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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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Enzyme Inhibition01:30

Enzyme Inhibition

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Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
78.5K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

8.2K
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...
8.2K
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

10.2K
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....
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Enzyme Kinetics01:19

Enzyme Kinetics

96.9K
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...
96.9K

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相关实验视频

Updated: Jul 10, 2025

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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通过最小化酶成本来探索竞争性的动态酶分配方案.

Shanshan Qi1,2, Gangsheng Wang3,4, Wanyu Li1,2

  • 1State Key Laboratory of Water Resources Engineering and Management, Wuhan University, Wuhan, 430072, China.

ISME communications
|November 21, 2023
PubMed
概括

微生物酶分配模型现在包括循环的多个酶组. 这种新模型优化了基于基质可用性的酶生产,最大限度地降低了代谢过程的成本.

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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
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科学领域:

  • 微生物生态学 微生物生态学
  • 生物地质化学生物地质化学
  • 计算建模计算建模

背景情况:

  • 酶分配是影响土壤生态化学循环的关键微生物特征.
  • 现有的微生物生态模型往往缺乏对多个酶组的综合酶分配方案.
  • 了解酶动力学对于预测生态系统对气候变化的反应至关重要.

研究的目的:

  • 为参与无机转换的六个酶组开发一种新的竞争性动态酶分配 (CODEAL) 方案.
  • 将该方案整合到微生物酶分解 (MEND) 模型中.
  • 研究酶分配策略如何影响微生物代谢效率和循环.

主要方法:

  • 开发一个动态的酶分配方案,为多个酶组提供时间变量的系数.
  • 在MEND模型中,在酶组之间实施相互竞争.
  • 利用基质和水平来指导酶分配并最大限度地降低代谢成本.

主要成果:

  • CODEAL 计划成功地模拟了六个酶组的循环分配.
  • 通过根据基质和水平分配酶来实现酶成本最小化.
  • 相对的基质可用性影响了酶生产和代谢流量之间的权衡.

结论:

  • CODEAL 方案提供了对酶介导的生物地球化学过程的更细致的理解.
  • 该模型通过结合竞争性酶分配来推进微生物生态建模.
  • 研究结果提供了有关循环动态和微生物适应策略的见解.