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Related Concept Videos

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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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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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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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

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Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
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Enzymes02:34

Enzymes

82.0K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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Related Experiment Video

Updated: Jul 26, 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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Rational design of allosteric switchable catalysts.

Tiezheng Pan1,2, Yaling Wang1, Xue Xue1

  • 1State Key Laboratory of Medicinal Chemical Biology Nankai University Tianjin China.

Exploration (Beijing, China)
|June 16, 2023
PubMed
Summary

Researchers are developing allosteric switchable catalysts inspired by natural enzymes. These synthetic catalysts offer precise control over reactions, expanding tools for chemical biology and biosensing applications.

Keywords:
allosterismmolecular machineself‐assemblysupramolecular catalysisswitchable catalyst

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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
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Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes
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Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks MOFs
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Area of Science:

  • Biomimetic chemistry
  • Catalysis
  • Chemical biology

Background:

  • Allosteric regulation is crucial for enzyme activity and cellular signaling.
  • Natural enzymes are often unstable and difficult to engineer for specific applications.
  • Controlling enzymatic networks is key to understanding and manipulating biological systems.

Purpose of the Study:

  • To review recent advancements in allosteric switchable catalysts.
  • To highlight the design strategies for creating synthetic catalysts with tunable activity.
  • To explore the application of these catalysts in chemical biology and biosensing.

Main Methods:

  • Summarizing recent literature on allosteric switchable catalysts.
  • Categorizing catalysts based on their structural scaffolds (single molecules, supramolecular complexes, self-assemblies).
  • Discussing design principles for tailoring biological and synthetic molecules into catalysts.

Main Results:

  • Allosterism concept extended beyond proteins to polymers, organic molecules, and supramolecular systems.
  • Demonstrated diverse design methods for creating controllable catalysts.
  • Highlighted the potential to mimic and control complex biological reactions.

Conclusions:

  • Allosteric switchable catalysts offer a powerful platform for controlling chemical reactions.
  • These synthetic catalysts can overcome limitations of natural enzymes.
  • Future applications include advanced biosensors, biomimetic cascades, and expanded chemical biology toolboxes.