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Related Concept Videos

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...
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...
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.
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...

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Related Experiment Video

Updated: May 29, 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

Dynamics and dissipation in enzyme catalysis.

Nicholas Boekelheide1, Romelia Salomón-Ferrer, Thomas F Miller

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Mail Code 127-72, Pasadena, CA 91125, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 21, 2011
PubMed
Summary
This summary is machine-generated.

Enzyme vibrations play a minimal role in hydride transfer. Protein fluctuations statistically gate the reaction barrier, rather than directly influencing it through nonlocal dynamics.

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR
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Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR

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Last Updated: May 29, 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

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR
10:54

Dissolution Dynamic Nuclear Polarization Instrumentation for Real-time Enzymatic Reaction Rate Measurements by NMR

Published on: February 23, 2016

Area of Science:

  • Biochemistry
  • Computational Biology
  • Enzyme Catalysis

Background:

  • Enzyme catalysis involves complex protein motions.
  • The role of enzyme vibrations in facilitating chemical reactions is debated.

Purpose of the Study:

  • To characterize the role of enzyme vibrations in dihydrofolate reductase (DHFR) hydride transfer.
  • To distinguish between statistical and dynamical correlations in enzyme motion.

Main Methods:

  • Quantized molecular dynamics (MD) simulations.
  • Sampling of reactive trajectories.
  • Analysis of protein-residue-reaction correlations.

Main Results:

  • Non-equilibrium dynamical coupling exists between protein residues and hydride transfer.
  • Dynamical correlations are short-range (4-6 Å).
  • Statistical correlations are long-range (nanometer-scale).

Conclusions:

  • Nonlocal vibrational dynamics play a minimal role in enzyme catalysis.
  • Protein fluctuations statistically modulate the reaction barrier.
  • Supports a gating model for enzyme catalysis.