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Updated: May 27, 2026

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Published on: September 13, 2014
Cooperativity in monomeric enzymes with single ligand-binding sites
Carol M Porter1, Brian G Miller
1Department of Chemistry and Biochemistry, 217 Dittmer Laboratory, Florida State University, Tallahassee, FL 32306-4390, USA.
Cooperativity, often seen in multi-subunit proteins, also occurs in single-subunit enzymes. This review explores the mechanisms and biological significance of cooperativity in monomeric enzymes.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Cooperativity is a fundamental biological principle influencing molecular interactions.
- Traditionally, cooperativity is associated with multimeric proteins and multiple binding sites.
- However, cooperativity can manifest in monomeric enzymes with single binding sites, challenging traditional views.
Purpose of the Study:
- To provide an overview of kinetic cooperativity in monomeric enzymes.
- To discuss proposed mechanisms underlying cooperativity in single-subunit enzymes.
- To highlight experimental techniques for studying this phenomenon and its biological relevance.
Main Methods:
- Literature review of existing studies on enzyme kinetics and cooperativity.
- Analysis of proposed mechanistic models for monomeric cooperativity.
- Discussion of modern experimental approaches, such as advanced spectroscopy and crystallography.
Main Results:
- Monomeric enzymes can exhibit non-Michaelis-Menten kinetics indicative of cooperativity.
- Several mechanisms, distinct from those in multimeric systems, are postulated for monomeric cooperativity.
- An updated list of monomeric enzymes suspected of cooperativity is presented.
Conclusions:
- Cooperativity is not exclusive to multimeric proteins and can be observed in monomeric enzymes.
- Understanding monomeric cooperativity offers new insights into enzyme regulation and function.
- Further research using modern techniques is crucial to elucidate the mechanisms and biological roles of cooperativity in single-subunit enzymes.
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