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関連する概念動画

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.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
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Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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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

Enzyme Kinetics

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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.
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...
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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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Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
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進化した正方形酵素/共因子ペア

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
まとめ
この要約は機械生成です。

研究者らは,血液タンパク質の機能を拡張するために,オートゴナルな酵素/ヘムペア戦略を開発した. 改造されたP450は非自然共因子を選択的に使用し,新しい化学反応を可能にします.

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科学分野:

  • 生物化学
  • バイオテクノロジー
  • 酵素工学

背景:

  • ヘモプロテインはヘム共因子を持つ重要な酵素である.
  • ヘモプロテインの機能を拡張するには,新しいコファクターの組み込み戦略が必要です.
  • サイトクロームP450は,しばしば新しい機能のために設計された多機能酵素です.

研究 の 目的:

  • ヘモプロテインの機能を拡張するための正交の酵素/ヘムペア戦略を開発する.
  • サイトクロームP450酵素 (P450BM3) を非本来のヘム誘導体の選択的組み込みのために設計する.
  • エンジニアリングされた酵素/共因子のペアの有用性を示すために.

主な方法:

  • ヘムを輸送するタンパク質の ChuA を利用して ヘムを輸入した.
  • 進化したP450BM3は,鉄デウテロポルフィリンIX (Fe-DPIX) を内在的ヘムに選択的に結合させる.
  • コファクター選択性の構造的基礎を解明するために,X線結晶学を用いた.
  • カーベノイド媒介サイクロプロパネーションで正対の触媒活性をテストした.

主要な成果:

  • エンジニアリングされたP450BM3は選択的にFe-DPIXをネイティブヘムと共に組み込みました.
  • 構造分析により,ステリックと結合相互作用によって選択性を授与する変異が明らかになった.
  • 進化した酵素/共因子ペアは,非自然なオレフィン・サイクロプロパネーションにおける活性を示した.
  • オートゴーナルな酵素/コファクター・ペアの生成に成功した.

結論:

  • 開発された戦略は,正交の酵素/共因子ペアの作成を可能にします.
  • このアプローチは,人工メタロ酵素のコファクター多様性を大幅に拡大します.
  • 設計されたシステムは,新しい生物触媒アプリケーションのためのプラットフォームを提供します.
  • 方法論は酵素工学と合成生物学でより広範な応用が期待されています.