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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

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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...
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Catalytically Perfect Enzymes01:07

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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.
 
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Introduction to Enzymes01:22

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The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
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Introduction to Enzyme Kinetics01:19

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
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Related Experiment Video

Updated: Dec 18, 2025

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
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A mechanistic view of enzyme evolution.

Gloria Yang1, Charlotte M Miton1, Nobuhiko Tokuriki1

  • 1Michael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.

Protein Science : a Publication of the Protein Society
|June 20, 2020
PubMed
Summary

Enzyme evolution enhances function through mutations that optimize latent activities. Understanding these molecular changes and common mechanisms is key for predicting and engineering improved enzyme catalysts.

Keywords:
activity-enhancing mutationsancestral sequence reconstructionconformational dynamicsconformational tinkeringdirected evolutionenzyme evolutionenzyme promiscuityenzyme-substrate complementaritymolecular mechanismssubstrate repositioning

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Enzyme function evolution often involves optimizing pre-existing promiscuous activities.
  • Understanding how mutations alter enzyme structure to enhance function is crucial for protein engineering.

Purpose of the Study:

  • To provide a mechanistic perspective on enzyme evolution by examining molecular changes underlying functional optimization.
  • To survey the prevalence and distribution of activity-enhancing mutations in protein structures.
  • To highlight common mechanisms mediating functional optimization across diverse enzymes.

Main Methods:

  • Review of recent studies on enzyme functional optimization.
  • Global survey of activity-enhancing mutations and their structural distribution.
  • Analysis of molecular solutions and common mechanisms in enzyme evolution.

Main Results:

  • Activity-enhancing mutations are prevalent and their distribution within protein structures varies.
  • Several common molecular mechanisms facilitate functional optimization in enzymes.
  • Evolutionary trajectories toward improved enzyme function can involve distinct mechanisms due to unique bottlenecks.

Conclusions:

  • Predicting mutations for enhanced enzyme activity is critical for rational protein design.
  • Identifying specific optimization mechanisms and tailoring engineering efforts to individual enzyme sequences improves catalyst generation.
  • Enzyme evolution is a complex process where distinct mechanisms emerge, necessitating sequence-specific engineering strategies.