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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

62.0K
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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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Updated: Nov 18, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

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Engineering an Allosteric Control of Protein Function.

Yashavantha L Vishweshwaraiah1, Jiaxing Chen1, Nikolay V Dokholyan1,2,3,4

  • 1Department of Pharmacology, Penn State College of Medicine, Hershey, Pennsylvania 17033-0850, United States.

The Journal of Physical Chemistry. B
|February 10, 2021
PubMed
Summary
This summary is machine-generated.

Engineered allosteric regulation precisely controls protein activity for diverse applications. This review covers identifying allosteric sites, regulatory strategies, and future challenges in protein engineering.

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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Allosteric regulation is crucial for biological processes, controlling protein function and activity.
  • Engineered allostery enables precise, rapid control of protein activity, with broad applications.

Purpose of the Study:

  • To review the concept of allosteric regulation in proteins.
  • To outline methods for identifying allosteric sites and pathways.
  • To discuss strategies and tools for engineered allosteric regulation.

Main Methods:

  • Literature review of allosteric regulation concepts.
  • Analysis of methods for allosteric site and pathway identification.
  • Overview of engineering strategies and tools for allosteric control.

Main Results:

  • Identified key approaches for allosteric site and pathway discovery.
  • Highlighted diverse protein classes regulated by allostery.
  • Summarized current strategies and tools for engineered allosteric regulation.

Conclusions:

  • Allosteric regulation is a powerful tool for controlling protein function.
  • Engineered allostery offers precise temporal control for various applications.
  • Future research should address current challenges in achieving robust allosteric regulation.