Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

11.7K
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...
11.7K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

10.3K
10.3K
Enzymes02:34

Enzymes

97.7K
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...
97.7K
Induced-fit Model01:13

Induced-fit Model

92.3K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
92.3K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

7.0K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
7.0K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

6.0K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
6.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Conformational flexibility of soybean lipoxygenase is coupled to crystal solvent content in serial crystallography.

bioRxiv : the preprint server for biology·2026
Same author

Computational Method for the Detection of Communication Pathways in Enzymes that Correlate with Experimentally Defined Thermal Activation Networks.

The journal of physical chemistry letters·2026
Same author

Correlated Motion-Based Residue Network Analysis Reveals the Distal Thermal Activation in Soybean Lipoxygenase.

bioRxiv : the preprint server for biology·2025
Same author

Dynamically Interacting Protein Networks Provide a Mechanism to Overcome the Enormous Intrinsic Barrier to Orotidine 5'-Monophosphate Decarboxylation.

ACS central science·2025
Same author

A Foundational Shift in Models for Enzyme Function.

Journal of the American Chemical Society·2025
Same author

Identification of Scaffold Specific Energy Transfer Networks in the Enthalpic Activation of Orotidine 5'-Monophosphate Decarboxylase.

bioRxiv : the preprint server for biology·2025
Same journal

Innate Immunity of Framework Nucleic Acids.

Accounts of chemical research·2026
Same journal

High-Performance CH-Series Non-Fullerene Acceptors for Organic Photovoltaics.

Accounts of chemical research·2026
Same journal

Design Principles for Negative Thermal Expansion in Two-Dimensional Materials.

Accounts of chemical research·2026
Same journal

Main Group Redox Catalysis: New Frontiers with Germanium and Tin.

Accounts of chemical research·2026
Same journal

Taming Irreversibility in sp<sup>2</sup>-Carbon-Conjugated COFs from Polycrystalline Powders to Single Crystals and Thin Films.

Accounts of chemical research·2026
Same journal

Electroactive Imidazolium Ionic Liquids in Organic Synthesis.

Accounts of chemical research·2026
See all related articles

Related Experiment Video

Updated: Apr 19, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

15.7K

Dynamically achieved active site precision in enzyme catalysis.

Judith P Klinman1

  • 1Department of Chemistry, Department of Molecular and Cell Biology, Institute of Quantitative Biology (QB3), University of California , Berkeley, California 94720, United States.

Accounts of Chemical Research
|December 25, 2014
PubMed
Summary
This summary is machine-generated.

Enzymes accelerate reactions through hydrogen tunneling and protein motions. A thermophilic alcohol dehydrogenase (ht-ADH) study reveals protein dynamics are crucial for optimal C-H activation and catalysis.

More Related Videos

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

12.1K
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

9.5K

Related Experiment Videos

Last Updated: Apr 19, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

15.7K
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

12.1K
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

9.5K

Area of Science:

  • Enzymology
  • Biophysical Chemistry
  • Protein Dynamics

Background:

  • Enzyme catalysis relies on understanding factors contributing to rate accelerations.
  • Hydrogen tunneling and protein motions are increasingly recognized as critical for enzyme function, beyond transition state stabilization.

Purpose of the Study:

  • To investigate the role of protein dynamics and hydrogen tunneling in the catalytic mechanism of a thermophilic alcohol dehydrogenase (ht-ADH).
  • To correlate protein motions with enzyme catalysis and understand the factors influencing C-H activation.

Main Methods:

  • Kinetic isotope effects to probe the chemical coordinate and C-H activation.
  • Site-directed mutagenesis to assess the impact of specific amino acid changes on catalysis.
  • Biophysical techniques including hydrogen/deuterium exchange and fluorescence spectroscopy to study protein dynamics.

Main Results:

  • A temperature-dependent transition in C-H activation was observed below 30 °C, distinguishing nonoptimal from optimal catalysis.
  • Mutagenesis studies showed that single amino acid changes can modulate or abolish this temperature-dependent transition.
  • Long-range protein motions, spanning approximately 30 Å from dimer to cofactor binding domains, were identified and correlated with catalysis.

Conclusions:

  • Protein conformational dynamics, including long-range motions, play a significant role in optimizing enzyme catalysis.
  • Hydrogen tunneling and the sampling of protein substates are critical for efficient C-H activation in ht-ADH.
  • Further research is needed to achieve higher spatial and temporal resolution of catalysis-linked protein motions.