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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

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

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...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

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...

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Related Experiment Video

Updated: Mar 20, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Dissecting Dynamic Allosteric Pathways Using Chemically Related Small-Molecule Activators.

George P Lisi¹, Gregory A Manley¹, Heidi Hendrickson¹

¹Department of Chemistry, Yale University, New Haven, CT 06520, USA.

Structure (London, England : 1993)

|May 31, 2016

Summary

This summary is machine-generated.

Allosteric activators enhance imidazole glycerol phosphate synthase (IGPS) activity by increasing conformational flexibility. Stronger ligands promote domain-wide loosening for maximum catalytic function.

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Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Imidazole glycerol phosphate synthase (IGPS) is a key enzyme in histidine biosynthesis.
Understanding its allosteric regulation is crucial for enzyme mechanism studies.

Purpose of the Study:

To elucidate the allosteric mechanism of heterodimeric IGPS.
To investigate the role of conformational flexibility in enzyme activation.

Main Methods:

Solution nuclear magnetic resonance (NMR) spectroscopy.
Molecular dynamics (MD) simulations.
Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments.

Main Results:

Ligand binding is entropically driven, with rate enhancements from 26- to 4,900-fold.
Allosteric activators stimulate domain-wide motions on the millisecond timescale.
Stronger allosteric ligands induce greater conformational flexibility in HisF, leading to enhanced activity.

Conclusions:

Conformational flexibility on the millisecond timescale is vital for intersubunit communication in IGPS.
The allosteric network is dispersed and effector-dependent.
Domain-wide loosening mediated by allosteric ligands maximizes catalytic activity.