Linear Eyring plots conceal a change in rate-limiting step in an enzyme reaction
Date
11/12/2018Metadata
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Abstract
The temperature dependence of psychrophilic and mesophilic (R)-3-hydroxybutyrate dehydrogenase steady-state rates yields nonlinear and linear Eyring plots, respectively. Solvent viscosity effects and multiple- and single-turnover pre-steady-state kinetics demonstrate that while product release is rate-limiting at high temperatures for the psychrophilic enzyme, either interconversion between enzyme-substrates and enzyme-products complexes or a step prior to it limits the rate at low temperature. Unexpectedly, a similar change in rate-limiting step is observed with the mesophilic en-zyme, where a step prior to chemistry becomes rate-limiting at low temperature. This observation may have implica-tions for past and future interpretation of temperature-rate profiles.
Citation
Machado , T F G , Gloster , T & da Silva , R G 2018 , ' Linear Eyring plots conceal a change in rate-limiting step in an enzyme reaction ' , Biochemistry , vol. 57 , no. 49 , pp. 6757-6761 . https://doi.org/10.1021/acs.biochem.8b01099
Publication
Biochemistry
Status
Peer reviewed
ISSN
0006-2960Type
Journal article
Rights
© 2018 American Chemical Society. This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Description
This work was supported by the Engineering and Physical Sciences Research Council (EPSRC) [grant number EP/L016419/1] via a CRITICAT Centre for Doctoral Training studentship to T.F.G.M. T.M.G. is a Wellcome Trust Career Development Fellow.Collections
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