AI Article Synopsis

  • Tryptophan synthase is an enzyme with complex allosteric interactions that regulate its two subunits' activity and ligand gate functions.
  • The enzyme carries out 13 different reaction steps, transferring intermediate products directly between its subunits.
  • A stochastic model developed in previous research is utilized to analyze the thermodynamics of tryptophan synthase, exploring the Gibbs energy landscape, entropy production, and information exchange due to allosteric interactions.

Article Abstract

The enzyme tryptophan synthase is characterized by a complex pattern of allosteric interactions that regulate the catalytic activity of its two subunits and opening or closing of their ligand gates. As a single macromolecule, it implements 13 different reaction steps, with an intermediate product directly channeled from one subunit to another. Based on experimental data, a stochastic model for the operation of tryptophan synthase has been earlier constructed [D. Loutchko, D. Gonze, and A. S. Mikhailov, J. Phys. Chem. B 120, 2179 (2016)]. Here, this model is used to consider stochastic thermodynamics of such a chemical nanomachine. The Gibbs energy landscape of the internal molecular states is determined, the production of entropy and its flow within the enzyme are analyzed, and the information exchange between the subunits resulting from allosteric cross-regulations and channeling is discussed.

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http://dx.doi.org/10.1063/1.4973544DOI Listing

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