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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...
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...
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...
Enzymes and Activation Energy01:13

Enzymes and Activation Energy

The activation energy (or free energy of activation), abbreviated as Ea, is the small amount of energy input necessary for all chemical reactions to occur. During chemical reactions, certain chemical bonds break, and new ones form. For example, when a glucose molecule breaks down, bonds between the molecule's carbon atoms break. Since these are energy-storing bonds, they release energy when broken. However, the molecule must be somewhat contorted to get into a state that allows the bonds to...

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Related Experiment Video

Updated: Jun 9, 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

Choreographing an enzyme's dance.

Janice Villali1, Dorothee Kern

  • 1Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, 415 South St., Waltham, MA 02454, USA.

Current Opinion in Chemical Biology
|September 9, 2010
PubMed
Summary
This summary is machine-generated.

Enzymes achieve high catalytic rates by navigating energy landscapes through coordinated protein movements. Transient hydrogen bonds help maintain energy during conformational changes, crucial for efficient enzyme catalysis.

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Modeling an Enzyme Active Site using Molecular Visualization Freeware

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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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Related Experiment Videos

Last Updated: Jun 9, 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

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
10:45

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
  • Structural Biology
  • Chemical Physics

Background:

  • Enzyme catalysis relies on complex energy landscapes, not just ground state structures.
  • Understanding the energy inventory is key to explaining enzyme rate enhancement.

Purpose of the Study:

  • Investigate enzyme transition pathways and energy landscapes.
  • Elucidate how proteins maintain structure during catalytic conformational changes.

Main Methods:

  • Time-resolved Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Molecular dynamics simulations.
  • Kinetic Isotope Effects (KIE) analysis.

Main Results:

  • Proteins dynamically sample conformations, avoiding unfolding during transitions.
  • Transient, non-native hydrogen bonds compensate for lost native contacts.
  • Protein atomic fluctuations, sensitive to distance, dictate reaction probabilities.

Conclusions:

  • Enzyme catalysis requires highly choreographed conformational sampling.
  • Protein dynamics and chemical integrity are essential for efficient enzymatic reactions.