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Updated: Jun 1, 2026
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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
Published on: February 18, 2014
Kinetics of allosteric activation
1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri, USA.
Methods in Enzymology
|May 26, 2011
Summary
Allosteric activators bind enzymes at sites separate from the active site, enhancing enzyme function. This review explores the kinetics of allosteric activation, focusing on enzymes with single substrate and allosteric effector binding sites.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Enzyme activity is often modulated by ligands binding to active or allosteric sites.
- Allosteric activation enhances enzyme function through distinct binding interactions.
- Monovalent cations are prominent activators in a wide range of enzymes.
Purpose of the Study:
- To review the fundamental kinetic principles of allosteric activation.
- To examine the specific case of an enzyme with separate substrate and allosteric effector binding sites.
- To elucidate the mechanisms underlying ligand-induced enzyme enhancement.
Main Methods:
- Theoretical kinetic analysis of enzyme systems.
- Modeling of enzyme-effector interactions.
- Review of established allosteric activation mechanisms.
Main Results:
- Allosteric activation requires effector binding at a site distinct from the substrate-binding active site.
- The kinetics of allosteric activation can be described by models considering separate binding events.
- Monovalent cations exemplify common allosteric activators.
Conclusions:
- Allosteric activation is a key regulatory mechanism in enzyme kinetics.
- Understanding distinct binding sites is crucial for comprehending enzyme modulation.
- The principles discussed apply broadly to enzymes regulated by allosteric effectors.
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