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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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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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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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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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Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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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.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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Induced-fit Model01:13

Induced-fit Model

81.1K
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.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
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Introduction to Enzymes01:22

Introduction to Enzymes

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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.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that...
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Related Experiment Video

Updated: Jul 18, 2025

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

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Thermodynamic principle to enhance enzymatic activity using the substrate affinity.

Hideshi Ooka1, Yoko Chiba2,3, Ryuhei Nakamura2,4

  • 1Biofunctional Catalyst Research Team, Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan. hideshi.ooka@riken.jp.

Nature Communications
|August 24, 2023
PubMed
Summary

Tuning the Michaelis-Menten constant (Km) to substrate concentration (S) enhances enzyme activity. This principle, derived from thermodynamics, appears to be followed by natural selection across diverse enzymes.

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Area of Science:

  • Biochemistry
  • Enzyme kinetics
  • Bio-engineering

Background:

  • Enzyme activity tuning is crucial for biotechnology and understanding biological systems.
  • The Michaelis-Menten equation is a foundational model, but lacks specific optimization guidelines.
  • Current understanding does not provide clear strategies for optimizing enzyme parameters for higher activity.

Purpose of the Study:

  • To establish a concrete guideline for optimizing enzyme parameters towards enhanced activity.
  • To demonstrate that aligning the Michaelis-Menten constant (Km) with substrate concentration (S) improves enzymatic performance.
  • To propose a generalizable thermodynamic principle for enhancing enzyme function.

Main Methods:

  • Mathematical derivation of enzyme activity optimization based on thermodynamic principles.
  • Assumption that thermodynamically favorable reactions possess higher rate constants.
  • Assumption of a fixed total driving force for reactions.

Main Results:

  • A novel guideline, Km ≈ S, was mathematically derived to enhance enzymatic activity.
  • Bioinformatic analysis of ~1000 enzymes showed consistency between Km and in vivo substrate concentrations.
  • This consistency suggests natural selection adheres to the proposed Km ≈ S principle.

Conclusions:

  • The principle Km ≈ S offers a generalizable strategy for enhancing enzyme activity.
  • Thermodynamic considerations provide a basis for optimizing enzyme kinetics.
  • Natural enzymes appear to have evolved under the constraint of matching Km to S for optimal function.