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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...

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

Regulation of Metabolism

Regulation of Metabolism

Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...

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Related Experiment Video

Updated: Jan 16, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Rewiring enzyme regulation: Allosteric drugs and predictive tools.

Vahap Gazi Fidan¹, Konuralp Ilim², Attila Gursoy³

¹Department of Chemical and Biological Engineering, Koç University, Istanbul 34450, Turkey.

Current Opinion in Structural Biology

|September 26, 2025

Summary

Allosteric modulation, a precise enzyme intervention strategy, is advancing rapidly. Computational and experimental methods are enhancing the identification and application of allosteric sites for drug discovery.

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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

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Last Updated: Jan 16, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Published on: October 4, 2024

Drug-induced Sensitization of Adenylyl Cyclase: Assay Streamlining and Miniaturization for Small Molecule and siRNA Screening Applications

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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

Area of Science:

Biochemistry and Pharmacology
Enzyme kinetics and regulation
Computational biology and drug discovery

Background:

Allosteric modulation offers a precise approach to targeting enzyme pathways.
Conventional drug design often focuses on orthosteric sites, limiting therapeutic options.
Understanding allosteric regulation is crucial for developing novel therapeutics.

Purpose of the Study:

To review emerging strategies for identifying and utilizing allosteric sites.
To highlight the integration of computational and experimental techniques in allosteric research.
To discuss the therapeutic potential of allosteric modulators in drug design.

Main Methods:

Computational frameworks integrating evolutionary, structural, and dynamic features with machine learning.
Perturbation-based simulations and network analyses for understanding allosteric regulation.
Deep mutational data and advanced experimental techniques for site validation.

Main Results:

Emerging computational strategies effectively identify and characterize allosteric sites.
Experimental validation confirms the relevance of cryptic and functionally important allosteric pockets.
FDA-approved allosteric modulators demonstrate successful therapeutic applications.

Conclusions:

Allosteric modulation is a powerful tool for precise enzymatic pathway intervention.
Integration of computational and experimental methods accelerates the discovery of allosteric modulators.
Allosteric drug design expands therapeutic targets beyond conventional binding sites, enhancing specificity and overcoming resistance.