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Multisite Enzymes as a Mechanism for Bistability in Reaction Networks.

Clarmyra Hayes, Elisenda Feliu1, Orkun S Soyer

  • 1Department of Mathematics, University of Copenhagen, DK-2100 Copenhagen, Denmark.

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|January 24, 2022
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Summary

Multisite enzymes, with multiple substrate binding sites, can generate bistable dynamics in biochemical reaction networks. Mathematical modeling reveals how enzyme kinetics and levels control this crucial biological switch.

Keywords:
enzyme kineticsmultistabilityphenotypic heterogeneityprotein engineeringreaction system dynamicssubstrate inhibitionsynthetic biology

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Area of Science:

  • Biochemistry
  • Systems Biology
  • Enzyme Kinetics

Background:

  • Multisite enzymes are crucial in biological pathways.
  • Understanding enzyme dynamics is key to cellular regulation.
  • Bistability is a fundamental biological switch mechanism.

Purpose of the Study:

  • To analyze the capacity of multisite enzymes to generate bistable dynamics.
  • To investigate reaction networks involving multisite enzymes.
  • To provide a framework for predicting and engineering enzyme bistability.

Main Methods:

  • Mathematical modeling of enzyme kinetics.
  • Analysis of reaction networks with substrate-product-substrate cycles and product consumption.
  • Derivation of analytical solutions for enzyme-substrate complex concentrations.

Main Results:

  • Multisite enzymes inherently possess the potential for bistable dynamics.
  • Analytical solutions reveal mechanistic understanding of bistability.
  • Specific enzyme kinetic parameters and enzyme levels can induce bistability.

Conclusions:

  • Enzyme binding and catalysis reactions in multisite enzymes create potential for bistability.
  • Parameter combinations guaranteeing bistability were derived.
  • Findings offer a basis for predicting and engineering bistability in multisite enzymes.