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相关概念视频

Cofactors and Coenzymes01:24

Cofactors and Coenzymes

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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
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Cofactors and Coenzymes01:27

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Cofactors and Coenzymes01:27

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Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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Enzyme Kinetics01:19

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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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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

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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.
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Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
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一种进化的正交酶/辅因子对

Evan W Reynolds1, Matthew W McHenry1, Fabien Cannac1

  • 1Department of Chemistry, University of North Carolina-Chapel Hill , 125 South Road, CB 3290, Chapel Hill, North Carolina 27599, United States.

Journal of the American Chemical Society
|August 31, 2016
PubMed
概括
此摘要是机器生成的。

研究人员开发了一种直角酶/血红蛋白对策来扩大血红蛋白的功能. 一个修改后的P450细胞染色体选择性地使用非自然的辅因子,使新的化学反应成为可能.

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科学领域:

  • 生物化学
  • 生物技术
  • 酶工程

背景情况:

  • 血红蛋白是具有血红配因子的关键酶.
  • 扩大血蛋白功能需要新的辅助因子结合策略.
  • 细胞染色体P450是多功能酶,通常用于新功能.

研究的目的:

  • 开发一个正交的酶/血对策略,以扩大血蛋白的功能.
  • 设计一种细胞P450酶 (P450BM3),以选择性地加入非本源的血衍生物.
  • 证明工程酶/辅助因子对在催化中的有用性.

主要方法:

  • 为了进口血红素衍生物,利用了混杂的血红素运输蛋白 ChuA.
  • 进化的P450BM3可选择性地将铁二甲氨酸IX (Fe-DPIX) 与内源性血结合.
  • 使用X射线结晶学来阐明辅因子选择性的结构基础.
  • 在碳化物中介循环化中测试直角对的催化活性.

主要成果:

  • 在本地血红素的存在下,工程P450BM3选择性地纳入Fe-DPIX.
  • 结构分析发现突变通过固体和结合相互作用赋予选择性.
  • 进化的酶/辅助因子对在非自然的烯酸环化中表现出活性.
  • 成功生成了一个正交的酶/辅因子对.

结论:

  • 开发的策略可以创建正交的酶/辅因子对.
  • 这种方法显著扩大了人工金属酶的辅因子多样性.
  • 这种工程系统为新的生物催化应用提供了一个平台.
  • 在酶工程和合成生物学中有望得到更广泛的应用.