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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 Transitions01:58

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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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Allosteric Proteins-ATCase01:19

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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

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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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Regulation of Metabolism01:19

Regulation of Metabolism

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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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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Updated: Jul 12, 2025

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

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All over or overall - Do we understand allostery?

Hagen Hofmann1

  • 1Department of Chemical and Structural Biology, Weizmann Institute of Science, Herzl St. 234, 76100 Rehovot, Israel.

Current Opinion in Structural Biology
|October 28, 2023
PubMed
Summary
This summary is machine-generated.

Allostery, crucial for cellular regulation, is explained by thermodynamic models. However, these models lack causal explanations, leaving a gap in understanding allosteric pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Systems Biology

Background:

  • Allostery is a fundamental mechanism regulating cellular processes.
  • Numerous models exist to explain allostery, but a comprehensive understanding remains elusive.
  • Current models primarily rely on thermodynamics, offering limited insight into causality.

Purpose of the Study:

  • To review and analyze popular allosteric models.
  • To identify similarities, differences, and limitations of existing thermodynamic models.
  • To highlight the need for a pathway-based, temporal description of allostery.

Main Methods:

  • Literature review of established allosteric models.
  • Comparative analysis of thermodynamic frameworks.
  • Discussion of the conceptual limitations of equilibrium-based models.

Main Results:

  • Thermodynamic models of allostery, while informative, contain inherent redundancies.
  • Existing models fail to fully satisfy the need for causal explanations in biological systems.
  • A significant gap exists in describing allostery as a dynamic, temporal sequence of events.

Conclusions:

  • Sixty years of research have not fully elucidated allosteric regulation due to reliance on thermodynamics.
  • A causal, pathway-based temporal description is essential for a complete understanding of allostery.
  • Future research should focus on integrating dynamic and temporal aspects into allosteric models.