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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 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

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

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Related Experiment Video

Updated: Nov 2, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Structurally distributed surface sites tune allosteric regulation.

James W McCormick^1,2, Marielle Ax Russo^1,2, Samuel Thompson³

¹The Green Center for Systems Biology, University of Texas Southwestern Medical Center, Dallas, United States.

|June 16, 2021

Summary

This summary is machine-generated.

Understanding mutations that control protein allostery is key for optimization. Few mutations significantly alter allosteric regulation, with beneficial ones found on the protein surface.

Keywords:

E. coli LOV2 allostery coevolution deep mutational scanning dihydrofolate reductase evolutionary biology molecular biophysics sectors structural biology

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Optimizing protein allosteric regulation is crucial for biological control.
Current knowledge of mutations tuning allostery is incomplete, hindering rational design.

Purpose of the Study:

To investigate the abundance and distribution of mutations affecting allosteric regulation.
To identify mutation patterns that can be leveraged for optimizing allosteric function.

Main Methods:

Saturation mutagenesis of a synthetic allosteric switch (Dihydrofolate reductase regulated by LOV2 domain).
High-throughput screening assay coupling enzyme activity to E. coli growth.
Analysis of 1548 viable Dihydrofolate reductase mutations' impact on allostery.

Main Results:

Fewer than 5% of mutations significantly impacted allosteric regulation.
Allosteric disruption mutations were localized near the LOV2 insertion site.
Allosteric enhancement mutations were distributed across the protein surface and improved dynamic range.

Conclusions:

Allosteric function can be optimized by targeted variations at surface-exposed sites.
A small fraction of mutations significantly influence allostery, with beneficial ones located on the surface.
Combining beneficial mutations leads to additive improvements in allosteric dynamic range.