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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...

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

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...

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,...

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...

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Related Experiment Video

Updated: Jun 24, 2026

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α

Published on: November 2, 2018

Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes

A E Aleshin¹, C Kirby, X Liu

¹Department of Biochemistry Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.

Journal of Molecular Biology

|February 25, 2000

Summary

This summary is machine-generated.

Researchers reveal the first crystal structures of the hexokinase I monomer, the brain

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Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Hexokinase I is a key enzyme in glycolysis, particularly in brain tissue.
The enzyme exists as a dimer at high concentrations, but monomeric properties are less understood.
Previous studies primarily focused on the hexokinase I monomer in solution.

Purpose of the Study:

To determine the first crystal structures of the human hexokinase I monomer.
To elucidate the binding sites and conformational changes associated with monomeric hexokinase I.
To provide insights into the allosteric regulation mechanism of hexokinase I.

Main Methods:

X-ray crystallography of mutant forms of recombinant human hexokinase I.
Analysis of ligand binding (glucose, glucose 6-phosphate, ADP) to distinct sites.
Observation of conformational changes upon ligand binding.

Main Results:

Novel crystal structures of the hexokinase I monomer were obtained.
High-affinity binding sites for glucose 6-phosphate, glucose, and ADP were identified in the N- and C-terminal halves.
A second ADP binding site at the active site (C-half) was revealed, inducing conformational changes.
Distinct conformational states of the C-half and rigid-body rotation of the N-half were observed.

Conclusions:

The study presents the first atomic-level view of the hexokinase I monomer.
Structural data suggest a mechanism for allosteric regulation involving distinct conformational states and domain movements.
These findings advance the understanding of glycolysis regulation in the brain.