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Allosteric Regulation

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

Allosteric Regulation

Allosteric Regulation

Allosteric Proteins-ATCase

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...

Ligand Binding and Linkage

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...

Cooperative Allosteric Transitions

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 Transitions

Cooperative Allosteric Transitions

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Related Experiment Video

Updated: May 1, 2026

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays

Published on: November 12, 2012

Computational approaches to mapping allosteric pathways.

Victoria A Feher¹, Jacob D Durrant¹, Adam T Van Wart¹

¹Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, USA.

Current Opinion in Structural Biology

|March 27, 2014

Summary

This summary is machine-generated.

Computational methods help reveal allosteric signaling pathways by analyzing atomistic details. These techniques are advancing drug discovery by identifying key residues for targeted therapies.

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Area of Science:

Biochemistry
Computational Biology
Pharmacology

Background:

Allosteric signaling involves remote site interactions affecting protein function.
Understanding these pathways is crucial for drug development.

Purpose of the Study:

To review computational techniques for elucidating allosteric signaling pathways.
To highlight the role of these methods in drug discovery.

Main Methods:

Dynamical network analysis
Topological and molecular dynamics methods
Hybrid computational approaches

Main Results:

Computational techniques elucidate allosteric signaling at the atomistic level.
Different methods excel at specific timescales and fluctuation magnitudes.
No single method is universally superior for pathway identification.

Conclusions:

Advanced computational methods are key to understanding allosteric mechanisms.
These techniques offer potential for identifying drug targets and advancing pharmacological interventions.