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

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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 pathway,...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Induced-fit Model01:13

Induced-fit Model

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 characteristics of...

You might also read

Related Articles

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

Sort by
Same author

Discordance Between Systemic Lupus Erythematosus Disease Activity Index Domain Weights and Their Association With Organ Damage Accrual.

Arthritis care & research·2026
Same author

The crystal structure of the toxin EspC from enteropathogenic <i>Escherichia coli</i> reveals the mechanism that governs host cell entry and cytotoxicity.

Gut microbes·2025
Same author

Molecular Interactions Required for Activation of Complement Component C2 Include Exosites Located on the Serine Protease Domain of C1s and Mannose-Binding Lectin Associated Protease-2.

Journal of immunology (Baltimore, Md. : 1950)·2024
Same author

Effect of a protease-activated receptor-2 antagonist (GB88) on inflammation-related loss of alveolar bone in periodontal disease.

Journal of periodontal research·2023
Same author

Mapping the binding site of C1-inhibitor for polyanion cofactors.

Molecular immunology·2020
Same author

Protease-associated import systems are widespread in Gram-negative bacteria.

PLoS genetics·2019
Same journal

Neuronal membrane organization by the submembranous spectrin-ankyrin scaffold: evolution, specialization and disease.

Biological chemistry·2026
Same journal

Golgi-associated membrane scaffolds: roles in health and disease.

Biological chemistry·2026
Same journal

Mechanistic insights on spatiotemporal control of Ras-signaling.

Biological chemistry·2026
Same journal

Cysteine cathepsin proteases in apicomplexan parasites.

Biological chemistry·2026
Same journal

Electron donating and withdrawing groups affect the antioxidant activity of 4'-aminochalcones on gentamicin-induced kidney cell injury.

Biological chemistry·2026
Same journal

CNKSR2 scaffold function in the mammalian nervous system.

Biological chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 24, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
09:47

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

Published on: May 25, 2018

Subsite cooperativity in protease specificity.

Natasha M Ng1, Robert N Pike, Sarah E Boyd

  • 1Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.

Biological Chemistry
|April 14, 2009
PubMed
Summary
This summary is machine-generated.

Subsite cooperativity in proteases influences substrate binding, impacting enzyme activity. Understanding this phenomenon is key to developing targeted protease pharmaceuticals.

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

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Related Experiment Videos

Last Updated: Jun 24, 2026

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
09:47

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

Published on: May 25, 2018

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

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Area of Science:

  • Enzymology
  • Molecular Biology
  • Biochemistry

Background:

  • Proteases are crucial enzymes involved in numerous biological processes.
  • Understanding protease active site function is essential for studying enzyme mechanisms.
  • Substrate specificity studies have revealed complex interactions within protease active sites.

Purpose of the Study:

  • To review the phenomenon of subsite cooperativity in proteases.
  • To highlight experimental techniques used to study subsite cooperativity.
  • To discuss potential future methods for examining subsite cooperativity.

Main Methods:

  • Literature review of studies on protease subsite cooperativity.
  • Analysis of kinetic and structural data related to enzyme-substrate interactions.
  • Discussion of experimental approaches for investigating enzyme active sites.

Main Results:

  • Subsite cooperativity, where binding at one site affects another, is a widespread phenomenon in proteases.
  • This cooperativity can occur between non-adjacent subsites.
  • It influences how proteases recognize and bind substrates.

Conclusions:

  • Subsite cooperativity significantly impacts protease substrate recognition and cleavage.
  • Further research into this phenomenon can lead to the development of novel protease-targeting drugs.
  • Comprehensive examination of subsite cooperativity is vital for advancing pharmaceutical development.