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Related Concept Videos

Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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...
Enzyme Kinetics01:19

Enzyme Kinetics

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...
Enzymes02:34

Enzymes

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...
Introduction to Enzymes01:22

Introduction to Enzymes

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 bind the substrates and convert them into products. Many enzymes also...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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...
Catalytically Perfect Enzymes01:07

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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Related Experiment Video

Updated: Jul 2, 2026

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

Concentration profiles near an activated enzyme.

Soohyung Park1, Noam Agmon

  • 1Institute of Chemistry and the Fritz Haber Research Center, The Hebrew University, Jerusalem 91904, Israel.

The Journal of Physical Chemistry. B
|September 2, 2008
PubMed
Summary

This study models enzyme kinetics, revealing how substrate concentration near an enzyme reaches a steady state. It highlights complex many-body effects influencing this process, particularly at the enzyme surface.

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Metabolic Mapping: Quantitative Enzyme Cytochemistry and Histochemistry to Determine the Activity of Dehydrogenases in Cells and Tissues
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Metabolic Mapping: Quantitative Enzyme Cytochemistry and Histochemistry to Determine the Activity of Dehydrogenases in Cells and Tissues

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Last Updated: Jul 2, 2026

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

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Published on: January 16, 2016

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone
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Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone

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Metabolic Mapping: Quantitative Enzyme Cytochemistry and Histochemistry to Determine the Activity of Dehydrogenases in Cells and Tissues
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Metabolic Mapping: Quantitative Enzyme Cytochemistry and Histochemistry to Determine the Activity of Dehydrogenases in Cells and Tissues

Published on: May 26, 2018

Area of Science:

  • Biochemistry and Biophysics
  • Chemical Kinetics
  • Computational Biology

Background:

  • Enzyme activation initiates substrate concentration changes near the enzyme.
  • Understanding these transient profiles is crucial for enzyme kinetics.
  • Previous models often simplified the complex many-body interactions involved.

Purpose of the Study:

  • To derive analytical expressions for steady-state and transient substrate concentration profiles.
  • To investigate the influence of many-body effects on diffusion-influenced reactions.
  • To analyze the behavior of substrate concentration at the enzyme surface under varying turnover rates.

Main Methods:

  • Application of modern theories for many-body effects in diffusion-influenced reactions.
  • Derivation of approximate analytical expressions for steady-state and Laplace transforms of transient profiles.
  • Validation using many-particle Brownian-dynamics simulations for Michaelis-Menten kinetics.

Main Results:

  • Analytical expressions show excellent agreement with Brownian-dynamics simulations.
  • Steady-state profiles exhibit hyperbolic dependence on distance, incorporating many-body effects.
  • Enzyme surface concentration shows a transition from monotonic decay (high turnover) to nonmonotonic behavior (slow turnover) due to reversible binding and diffusion.

Conclusions:

  • The study provides accurate analytical models for enzyme-substrate concentration dynamics.
  • Many-body effects significantly impact substrate concentration profiles, especially at the enzyme surface.
  • A critical turnover rate constant for the observed transition can be estimated under specific conditions.