Abstract
The study of enzyme reaction mechanisms is fundamentally important to our understanding of biochemistry, cellular metabolism, and drug development. This Perspective focuses on the use of kinetic solvent viscosity effects (KSVEs) to study enzyme reactions. This technique is easily implemented and uses steady-state kinetic analyses to probe whether substrate binding is diffusion-controlled and whether product release is the rate-limiting step in the catalytic cycle. In addition, KSVEs can identify isomerization steps that are important for catalysis. The use of KSVEs in combination with other techniques, such as kinetic isotope effects, pH effects, and site-directed mutagenesis, can provide a detailed view of the mechanism of enzyme action. We present the basic theory, important experimental considerations, and potential outcomes and briefly discuss some examples from the literature. The derivation of the equations that are important for data analysis is also presented.
Recommended Citation
G. Gadda and P. Sobrado, "Kinetic Solvent Viscosity Effects as Probes for Studying the Mechanisms of Enzyme Action," Biochemistry, vol. 57, no. 25, pp. 3445 - 3453, American Chemical Society, Jun 2018.
The definitive version is available at https://doi.org/10.1021/acs.biochem.8b00232
Department(s)
Chemistry
International Standard Serial Number (ISSN)
1520-4995; 0006-2960
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 American Chemical Society, All rights reserved.
Publication Date
26 Jun 2018
PubMed ID
29874467
Comments
National Science Foundation, Grant 1506206