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Related Concept Videos

Heterogeneous Catalysis01:22

Heterogeneous Catalysis

Heterogeneous catalysis involves a catalyst in a different phase from the reactants. It is a process where the catalyst and the reactants are in distinct phases, typically solid and gas or liquid.Most heterogeneous catalysts are metals, metal oxides, or acids. The list includes transition metals like iron (Fe), cobalt (Co), nickel (Ni), palladium (Pd), platinum (Pt), chromium (Cr), manganese (Mn), tungsten (W), silver (Ag), and copper (Cu). These metals possess partially vacant d orbitals that...
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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 a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

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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.
Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion. The...
Catalysis02:50

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Engineering AaADH1 for enhanced catalytic efficiency and solubility via substrate tunnel modulation.

Chenyu Wang1, Xiao Feng2, Lixia Zong3

  • 1NHC Key Laboratory of Biotechnology of Antibiotics, Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China; School of Pharmacy, North China University of Science and Technology, Tangshan, Hebei 063210, China.

Enzyme and Microbial Technology
|July 8, 2026
PubMed
Summary

Protein engineering enhanced Artemisinic alcohol dehydrogenase 1 (AaADH1) for artemisinic acid production. Key mutations improved enzyme activity and expression, paving the way for industrial applications.

Keywords:
Alanine scanningArtemisinic alcohol dehydrogenaseCatalytic efficiencyMolecular Dynamics SimulationSubstrate Tunnel

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Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Published on: October 18, 2019

Area of Science:

  • Biochemistry
  • Enzyme Engineering
  • Drug Discovery

Background:

  • Artemisinic alcohol dehydrogenase 1 (AaADH1) is crucial for artemisinic acid biosynthesis, a precursor to the antimalarial drug artemisinin.
  • Current limitations in AaADH1's catalytic activity and yield hinder its industrial use.

Purpose of the Study:

  • To improve the enzymatic properties of AaADH1 through structure-guided protein engineering.
  • To enhance catalytic activity, efficiency, and expression levels for industrial artemisinic acid production.

Main Methods:

  • Structure-guided protein engineering and alanine scanning mutagenesis were used to identify key residues.
  • Saturation mutagenesis at position 366 and molecular dynamics simulations were performed.
  • Enzymatic assays and expression level analysis were conducted to evaluate mutant performance.

Main Results:

  • The L366A mutant showed a 30% increase in activity and a 53% enhancement in catalytic efficiency (kcat/KM).
  • Expression levels of L366A were 5-fold higher than the wild type (WT).
  • Further mutations at L366 (L366V, L366I, L366F) increased kcat/KM by up to 100% and improved pocket flexibility and local structure stability.

Conclusions:

  • Mutations at L366 significantly enhance AaADH1's activity, catalytic efficiency, and expression.
  • Protein engineering provides a rational approach to optimize AaADH1 for industrial artemisinic acid production.
  • These findings offer a framework for developing improved enzymes for pharmaceutical precursor synthesis.