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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

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

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

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...

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Related Experiment Video

Updated: Mar 25, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Controlling Allosteric Networks in Proteins.

Nikolay V Dokholyan¹

¹Department of Biochemistry and Biophysics, University of North Carolina , Chapel Hill, North Carolina 27599, United States.

Chemical Reviews

|February 20, 2016

Summary

This summary is machine-generated.

Protein allostery, conformational changes from ligand binding, is key to regulation and drug discovery. Manipulating allosteric sites offers therapeutic strategies, as shown by rescuing cystic fibrosis transmembrane conductance regulator function.

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Last Updated: Mar 25, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Published on: October 4, 2024

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Allosteric transition, a protein's conformational change upon ligand binding, is fundamental to biological regulation.
Allostery is increasingly leveraged for controlling protein activity and function.

Purpose of the Study:

To review the origins and significance of protein allostery.
To explore methods for identifying allosteric pathways and engineering proteins for functional control.
To demonstrate therapeutic potential through a case study.

Main Methods:

Review of physical and evolutionary origins of allostery.
Description of computational and experimental approaches for identifying allosteric pathways.
Protein engineering strategies targeting allosteric sites.

Main Results:

Allosteric pathways connect ligand-binding sites to functional sites, mediating conformational changes.
Protein engineering can modulate allosteric sites to control protein function.
A synergistic approach rescued the function of the cystic fibrosis transmembrane conductance regulator.

Conclusions:

Allosteric manipulation is a powerful tool for understanding molecular mechanisms and developing therapeutics.
Targeting allosteric sites offers a route to rescue protein function and treat diseases.
Allosteric control facilitates the interrogation of complex cellular processes.