Solution NMR Spectroscopy for the Study of Enzyme Allostery

Allostery is a ubiquitous biological regulatory process in which distant binding sites within a protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions play essential roles in many enzymological mechanisms, often facilitating formation of enzyme–substrate complexes...

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Bibliographic Details
Published in:Chemical reviews 2016-06, Vol.116 (11), p.6323-6369
Main Authors: Lisi, George P, Loria, J. Patrick
Format: Article
Language:English
Subjects:
Allosteric Regulation
Binding Sites
Biomolecules
Enzymes
Enzymes - chemistry
Enzymes - metabolism
Fluctuation
Government regulations
Hemoglobins - chemistry
Mathematical models
Molecules
NMR
NMR spectroscopy
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Solutions - chemistry
Thermodynamics
Transformations
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Summary:Allostery is a ubiquitous biological regulatory process in which distant binding sites within a protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions play essential roles in many enzymological mechanisms, often facilitating formation of enzyme–substrate complexes and/or product release. Thus, elucidating the forces that drive allostery is critical to understanding the complex transformations of biomolecules. Currently, a number of models exist to describe allosteric behavior, taking into account energetics as well as conformational rearrangements and fluctuations. In the following Review, we discuss the use of solution NMR techniques designed to probe allosteric mechanisms in enzymes. NMR spectroscopy is unequaled in its ability to detect structural and dynamical changes in biomolecules, and the case studies presented herein demonstrate the range of insights to be gained from this valuable method. We also provide a detailed technical discussion of several specialized NMR experiments that are ideally suited for the study of enzymatic allostery.
ISSN:0009-2665
1520-6890
DOI:10.1021/acs.chemrev.5b00541