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Updated: Jun 29, 2025

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

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結晶学的に強化されたコンフォームショナルサンプリングを用いた効率的な人工酵素の設計

Rojo V Rakotoharisoa1,2, Behnoush Seifinoferest3, Niayesh Zarifi1,2

  • 1Department of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.

Journal of the American Chemical Society
|March 27, 2024
PubMed
まとめ

コンピューターによる設計は 人工酵素の効率を大幅に高めます この方法では 構造的なアンサンブルを使って 高活性な酵素を作り出し 広範なスクリーニングなしに 伝統的な誘導進化を上回ります

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Catalytically Perfect Enzymes

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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