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Multisite enzymes as a mechanism for bistability in reaction networks

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Hayes, Clarmyra, Feliu, Elisenda and Soyer, Orkun S. (2022) Multisite enzymes as a mechanism for bistability in reaction networks. ACS Synthetic Biology, 11 (2). pp. 596-607. doi:10.1021/acssynbio.1c00272

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Official URL: http://dx.doi.org/10.1021/acssynbio.1c00272

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Abstract

Here, we focus on a common class of enzymes that have multiple substrate binding sites (multisite enzymes) and analyze their capacity to generate bistable dynamics in the reaction networks that they are embedded in. These networks include both substrate–product–substrate cycles and substrate-to-product conversion with subsequent product consumption. Using mathematical techniques, we show that the inherent binding and catalysis reactions arising from multiple substrate–enzyme complexes create a potential for bistable dynamics in such reaction networks. We construct a generic model of an enzyme with n-substrate binding sites and derive an analytical solution for the steady-state concentration of all enzyme–substrate complexes. By studying these expressions, we obtain a mechanistic understanding of bistability, derive parameter combinations that guarantee bistability, and show how changing specific enzyme kinetic parameters and enzyme levels can lead to bistability in reaction networks involving multisite enzymes. Thus, the presented findings provide a biochemical and mathematical basis for predicting and engineering bistability in multisite enzymes.

Item Type: Journal Article
Subjects: Q Science > QH Natural history
Q Science > QP Physiology
T Technology > TP Chemical technology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Synthetic biology , Enzyme kinetics, Protein engineering, Enzymes -- Stabilit, Cells -- Mathematical models
Journal or Publication Title: ACS Synthetic Biology
Publisher: American Chemical Society
ISSN: 2161-5063
Official Date: 18 February 2022
Dates:
DateEvent
18 February 2022Published
24 January 2022Available
31 July 2021Accepted
Volume: 11
Number: 2
Page Range: pp. 596-607
DOI: 10.1021/acssynbio.1c00272
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Copyright Holders: © 2022 The Authors. Published by American Chemical Society
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
NNF18OC0052483 Danmarks Grundforskningsfondhttp://dx.doi.org/10.13039/501100001732
NNF18OC0052483 Novo Nordiskhttp://dx.doi.org/10.13039/501100004191
EP/L016494/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
EP/L016494/1 [EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266

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