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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.
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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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Feedback Inhibition00:46

Feedback Inhibition

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Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
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Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

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Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
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Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:29

Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

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Indirect-acting cholinergic agonists are agents that interact with the acetylcholinesterase enzyme in the synaptic cleft, preventing the breakdown of acetylcholine into choline and acetate. Consequently, the concentration of acetylcholine in the synaptic cleft increases. These agonists can be classified into reversible and irreversible inhibitors based on their duration of action.
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
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  2. 可逆光开关抑制剂在失衡的酶反应中产生超敏感性
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  2. 可逆光开关抑制剂在失衡的酶反应中产生超敏感性

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Determination of the Photoisomerization Quantum Yield of a Hydrazone Photoswitch
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Determination of the Photoisomerization Quantum Yield of a Hydrazone Photoswitch

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可逆光开关抑制剂在失衡的酶反应中产生超敏感性

Michael Teders1, Aleksandr A Pogodaev1, Glenn Bojanov1

  • 1Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.

Journal of the American Chemical Society
|April 12, 2021

在PubMed 上查看摘要

概括
此摘要是机器生成的。

科学家们开发了一种使用光来控制酶活动的新方法, 这一突破使得生物化学信号的精确调节和频率过成为可能.

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科学领域:

  • 生物化学
  • 合成生物学
  • 化学工程

背景情况:

  • 超敏感性是生物网络的一个关键特性,
  • 具有超灵敏性的合成网络可以使新型生命材料成为可能.

研究的目的:

  • 开发一种使用光线可逆控制酶活性的通用和模块化策略.
  • 用可光切换抑制剂在失衡的酶系统中证明过敏性.

主要方法:

  • 合成的可光切换抑制剂 (PI) 用于蛋白酶α-chymotrypsin使用染色体/战头策略.
  • 在失衡条件下的微流体流设置中研究了酶反应.
  • 用光脉冲辐射连续动的水箱反应器,以切换抑制剂光异构体.

主要成果:

  • 发现PIs在光异构体之间的抑制常数有显著差异.
  • 在照射光线时观察到过敏的酶活性反应.
  • 通过改变光脉冲序列来证明输入信号的频率过.

结论:

  • 开发的策略允许对酶动态进行可逆和可调节的控制.
  • 这种方法使酶可编程连接到多种网络拓中.
  • 这些发现为设计具有可控性质的先进生命材料铺平了道路.