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Related Concept Videos

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 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...
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...
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...
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...

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Related Experiment Video

Updated: May 12, 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

Structured crowding and its effects on enzyme catalysis.

Buyong Ma1, Ruth Nussinov

  • 1Basic Science Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, Frederick National Laboratory for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA, mabuyong@mail.nih.gov.

Topics in Current Chemistry
|April 11, 2013
PubMed
Summary
This summary is machine-generated.

Macromolecular crowding significantly impacts enzyme catalysis by altering protein dynamics and interactions. Structured cellular environments, unlike uniform crowding, may enhance enzyme efficiency and specificity.

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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)
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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

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Last Updated: May 12, 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

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)
08:25

Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)

Published on: January 17, 2020

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

Area of Science:

  • Biochemistry
  • Cell Biology
  • Enzyme Kinetics

Background:

  • Macromolecular crowding influences diffusion rates, interaction equilibria, and protein dynamics.
  • These effects collectively contribute to enzyme catalysis within cellular environments.

Purpose of the Study:

  • To elucidate how crowding biases enzyme conformational changes and dynamics, thereby affecting catalysis.
  • To differentiate between uniform and structured crowding environments and their impact on enzymes.

Main Methods:

  • Review of studies utilizing artificial crowding agents and in vivo-like conditions.
  • Analysis of the correlation between protein dynamics and function in crowded settings.

Main Results:

  • Crowding affects protein-protein and protein-substrate interactions, influencing enzyme catalysis.
  • Structured crowding, found in cellular environments, may offer functional modulation with potentially lower thermal stability perturbation.
  • Enzyme sensitivity to crowding depends on the landscape of their free energy states.

Conclusions:

  • Cellular environments are inherently structured, influencing macromolecular interactions and enzyme function.
  • Crowders may actively participate in allosteric regulation, playing functional roles.
  • Structured cellular crowding can potentially enhance enzyme efficiency and specificity.