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相关概念视频

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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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.
 
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Introduction to Enzyme Kinetics01:19

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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.
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Enzymes02:34

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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.
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在酶催化,进化和设计背后的全球动态.

Burcu Aykac Fas1, Zeynep Erge Akbas Buz1, Turkan Haliloglu1

  • 1Department of Chemical Engineering, Bogazici University, Istanbul, Turkey; Polymer Research Center, Bogazici University, Istanbul, Turkey.

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概括
此摘要是机器生成的。

酶使用大规模的运动和性相互作用来驱动催化. 了解这些动态,可以了解酶的功能,并指导创新的酶设计.

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科学领域:

  • 生物化学 生物化学
  • 结构生物学 结构生物学
  • 酶学 是一种酶学.

背景情况:

  • 酶是动态分子,其功能取决于形状变化.
  • 了解不同时间尺度上的酶动态的协调对于解释催化作用至关重要.
  • 酶动力学和生物化学活性之间的相互作用是复杂的,并未完全理解.

研究的目的:

  • 审查大规模集体运动在酶催化中的作用.
  • 要突出域移动和全相互作用如何促进酶功能的作用.
  • 探索动态机械化学合对酶设计的影响.

主要方法:

  • 这篇迷你综述综合了有关酶动态的现有研究.
  • 专注于大规模的运动,包括域级移位和基于链的重新排列.
  • 检查了动力学,性调节和催化机制之间的联系.

主要成果:

  • 大规模的集体运动对于基质的识别,转化和释放至关重要.
  • 这些运动是由多方向的全质相互作用驱动和传播的.
  • 动态机械化学合反映了酶功能的进化适应.

结论:

  • 酶催化在根本上与大规模的结构动力学有关.
  • 所有的交互作用在协调这些动态方面发挥着关键作用.
  • 了解酶动力学为设计具有增强功能的新型酶提供了一个框架.