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Related Concept Videos

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.
 
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Turnover Number and Catalytic Efficiency01:19

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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.
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Enzyme Kinetics01:19

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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.
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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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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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Factors Affecting Activity Coefficient01:17

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The extended Debye-Hückel equation indicates that the activity coefficient of an ion in an aqueous solution at 25°C depends on three partially interdependent properties: the ionic strength of the solution, the charge of the ion, and the ion size. 
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
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Exploring the Evolution-Coupling Hypothesis: Do Enzymes' Performance Gains Correlate with Increased Dissipation?

Davor Juretić1

  • 1Faculty of Science, University of Split, Ruđera Boškovića 33, 21000 Split, Croatia.

Entropy (Basel, Switzerland)
|April 26, 2025
PubMed
Summary
This summary is machine-generated.

Biological evolution drives life through specialized enzymes that enhance free-energy dissipation. This process, crucial for thermodynamic evolution, optimizes enzyme function and efficiency.

Keywords:
catalytic efficiencydissipationentropy productionevolutiongeneralist enzymeskinetic constantsscaling lawsspecialized enzymesstochastic noiseturnover number

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Area of Science:

  • Biophysics
  • Biochemistry
  • Evolutionary Biology

Background:

  • Divergent views exist on dissipation's role in living systems, from negligible to essential.
  • Thermodynamic evolution, indicated by entropy production, is often overlooked in biological contexts.

Purpose of the Study:

  • To investigate the relationship between enzyme kinetics, dissipation, and biological evolution.
  • To quantify enzyme-associated dissipation under steady-state conditions.

Main Methods:

  • Calculated enzyme-associated dissipation using minimalistic models of enzyme kinetics.
  • Analyzed enzyme kinetics with known microscopic rate constants under steady-state conditions.

Main Results:

  • Dissipation is proportional to enzyme turnover number.
  • A log-log power-law relationship exists between dissipation and catalytic efficiency.
  • Highly specialized enzymes show the highest dissipation, indicating evolutionary advancement.

Conclusions:

  • Biological evolution enhances free-energy dissipation via specialized enzymes.
  • Enzyme evolution likely progresses from generalist to specialist with increased dissipation.
  • Stochastic noise can optimize enzyme kinetics beyond observed values.