ArticleJournal of biological physics2017
Is the catalytic activity of triosephosphate isomerase fully optimized? An investigation based on maximization of entropy production.
Article in Journal of biological physics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Enzyme Catalytic Parameters and Evolution Across the Dissipation Plane.International journal of molecular sciences · 2026Review
- Exploring the Evolution-Coupling Hypothesis: Do Enzymes' Performance Gains Correlate with Increased Dissipation?Entropy (Basel, Switzerland) · 2025Article
- Theoretical Improvements in Enzyme Efficiency Associated with Noisy Rate Constants and Increased Dissipation.Entropy (Basel, Switzerland) · 2024Article
- Self-Organization of Enzyme-Catalyzed Reactions Studied by the Maximum Entropy Production Principle.International journal of molecular sciences · 2023Article
- Maximum Entropy Production Theorem for Transitions between Enzyme Functional States and Its Applications.Entropy (Basel, Switzerland) · 2019Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Triosephosphate isomerase (TIM) is often described as a fully evolved housekeeping enzyme with near-maximal possible reaction rate. The assumption that an enzyme is perfectly evolved has not been easy to confirm or refute. In this paper, we use maximization of entropy production within known constraints to examine this assumption by calculating steady-state cyclic flux, corresponding entropy production, and catalytic activity in a reversible four-state scheme of TIM functional states. The maximal entropy production (MaxEP) requirement for any of the first three transitions between TIM functional states leads to decreased total entropy production. Only the MaxEP requirement for the product (R-glyceraldehyde-3-phosphate) release step led to a 30% increase in enzyme activity, specificity constant k
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