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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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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...
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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...
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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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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: Mar 6, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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An evolution-based strategy for engineering allosteric regulation.

David Pincus1, Orna Resnekov, Kimberly A Reynolds

  • 1Whitehead Institute for Biomedical Research, Cambridge, MA 02142, United States of America. All authors contributed equally and are listed alphabetically.

Physical Biology
|March 8, 2017
PubMed
Summary
This summary is machine-generated.

We developed a new method called Rational Engineering of Allostery at Conserved Hotspots (REACH) to engineer novel protein regulation. This approach exploits evolutionary conserved sites to control protein function for applications in biosensing and drug design.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Synthetic Biology
  • Protein Engineering

Background:

  • Allosteric regulation controls protein activity on rapid timescales (milliseconds to seconds) within cells.
  • Engineering synthetic allosteric systems has significant potential for biosensors, synthetic signaling, and pharmaceutical development.
  • Existing methods for engineering allostery are limited.

Purpose of the Study:

  • To present a generalizable approach for introducing novel allosteric regulation into proteins.
  • To exploit evolutionarily conserved 'allosteric hotspots' within protein structures.
  • To enable the rewiring of cellular processes for novel input responses.

Main Methods:

  • Utilized Statistical Coupling Analysis (SCA) to identify potential allosteric hotspots on protein surfaces.
  • Developed and implemented experimental assays to validate the functionality of identified hotspots.
  • Employed a toolkit of allosteric modulators to influence endogenous cellular circuitry.

Main Results:

  • Successfully identified and validated allosteric hotspots using the REACH approach.
  • Demonstrated the potential to engineer novel regulatory functions into proteins.
  • Established a framework for creating synthetic allosteric control in biological systems.

Conclusions:

  • The Rational Engineering of Allostery at Conserved Hotspots (REACH) method provides a powerful strategy for protein engineering.
  • REACH enables the introduction of precise, tunable allosteric control into proteins by leveraging evolutionary information.
  • This approach has broad applicability for designing novel biological functions and therapeutic agents.