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Related Concept Videos

Catalysis02:50

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
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 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...
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...
Catalysis01:27

Catalysis

Catalysis influences the rate of chemical reactions by providing an alternative reaction pathway with lower activation energy. A catalyst speeds up a reaction, but it is not consumed during the process. The fundamental principle of catalysis is the ability of a catalyst to alter the reaction mechanism, often introducing a more efficient pathway than the uncatalyzed process.In a catalyzed reaction, the catalyst participates directly in the reaction mechanism. It interacts with reactants to form...

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Related Experiment Video

Updated: Jul 7, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Enzyme dynamics during catalysis.

Elan Zohar Eisenmesser1, Daryl A Bosco, Mikael Akke

  • 1Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.

Science (New York, N.Y.)
|February 23, 2002
PubMed
Summary
This summary is machine-generated.

Enzyme internal protein dynamics are crucial for catalysis. This study reveals active site conformational fluctuations in cyclophilin A during catalysis, correlating with substrate turnover rates and enabling reaction trajectory prediction.

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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

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Related Experiment Videos

Last Updated: Jul 7, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
14:27

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity

Published on: August 19, 2013

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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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

Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Protein Dynamics

Background:

  • Enzymatic catalysis is intrinsically linked to internal protein dynamics.
  • Understanding enzyme motions during substrate turnover is essential for elucidating catalytic mechanisms.
  • Specific enzyme dynamics related to catalytic activity remain largely uncharacterized.

Purpose of the Study:

  • To investigate enzyme dynamics at atomic resolution during catalysis.
  • To identify and characterize conformational fluctuations in the enzyme's active site.
  • To correlate enzyme motion rates with substrate turnover rates.

Main Methods:

  • Utilized nuclear magnetic resonance (NMR) relaxation methods for studying enzyme dynamics.
  • Applied atomic resolution techniques to analyze protein motion.
  • Focused on the enzyme cyclophilin A during its catalytic action.

Main Results:

  • Detected conformational fluctuations of the active site of cyclophilin A on a microsecond timescale during catalysis.
  • Observed a strong correlation between the rates of these conformational dynamics and the microscopic rates of substrate turnover.
  • Provided data that, combined with structural information, allows for prediction of the reaction trajectory.

Conclusions:

  • Internal protein dynamics, specifically active site fluctuations, play a significant role in enzymatic catalysis.
  • The identified microsecond-scale dynamics are directly linked to the enzyme's catalytic efficiency.
  • This research offers a pathway to predict enzymatic reaction trajectories based on dynamic properties.