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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 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...

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...

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

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 a mild...

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 pathway,...

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Engineering an allosteric binding site for aminoglycosides into TEM1-β-Lactamase.

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Related Experiment Video

Updated: Jun 18, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Engineering allosteric regulation into biological catalysts.

Jacques Fastrez¹

¹Laboratoire d'Ingénierie de Protéines et des Peptides, Louvain-la-Neuve, Belgium. jacques.fastrez@uclouvain.be

Chembiochem : a European Journal of Chemical Biology

|November 26, 2009

Summary

This summary is machine-generated.

Scientists are engineering biological catalysts, like enzymes and ribozymes, for allosteric regulation. This review explores strategies for creating these modified catalysts, enhancing their control and applications.

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Last Updated: Jun 18, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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

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Published on: February 18, 2014

Area of Science:

Biochemistry and Molecular Biology
Synthetic Biology

Background:

Enzymes and ribozymes are biological catalysts.
Allosteric regulation controls enzyme activity via effector molecules binding to sites distinct from the active site.
Understanding allosteric mechanisms is crucial for catalyst design.

Purpose of the Study:

To review recent advancements in allosteric regulation theories.
To compare strategies for engineering allosteric regulation into enzymes and ribozymes.
To highlight applications of engineered biological catalysts.

Main Methods:

Summarizing recent progress in allosteric regulation theories.
Describing and comparing engineering strategies for allosteric regulation.
Reviewing applications of engineered catalysts.

Main Results:

Allosteric regulation mechanisms are continually refined.
Rational design and directed evolution enable engineering of allosteric control in enzymes.
Ribozymes can also be successfully engineered for allosteric regulation.

Conclusions:

Engineered enzymes and ribozymes with allosteric control offer new possibilities.
These redesigned catalysts have diverse applications.
Further research into allosteric regulation engineering is warranted.