# Enzyme Catalytic Parameters and Evolution Across the Dissipation Plane

**Authors:** Davor Juretić, Branka Bruvo Mađarić

PMC · DOI: 10.3390/ijms27041709 · International Journal of Molecular Sciences · 2026-02-10

## TL;DR

This review explores how enzyme performance is shaped by thermodynamic constraints and evolution, revealing a connection between dissipation, efficiency, and evolutionary divergence.

## Contribution

The paper introduces the concept of a 'dissipation plane' linking enzyme kinetics, thermodynamics, and evolution through entropy production.

## Key findings

- Enzyme catalytic parameters are systematically linked to energetic dissipation.
- Enzymes exhibit correlated increases in dissipation, evolutionary divergence, and performance.
- Dissipation serves as a unified parameter connecting thermodynamics and evolution.

## Abstract

Enzyme performance parameters, including the turnover number and specificity constant, exhibit remarkable diversity due to biological evolution and natural selection. In some bacterial and human enzymes, catalytic efficiencies approach fundamental physical limits, underscoring the importance of physical constraints on enzymatic function. A deeper understanding of these constraints, particularly in far-from-equilibrium irreversible processes, is therefore essential for rational enzyme engineering. Such constraints are most naturally addressed within the frameworks of nanothermodynamics and stochastic thermodynamics, which remain relatively unfamiliar to much of the molecular biology community. Recent theoretical and experimental advances indicate that classical enzyme kinetic parameters are not independent, but are systematically linked to energetic dissipation. In particular, enzymes appear to occupy a characteristic dissipation plane defined by entropy production, reflecting the coupled influence of thermodynamic principles and evolutionary selection. In this review, we synthesize evidence across diverse enzyme families demonstrating correlated increases in housekeeping dissipation, evolutionary divergence, and enzymatic performance. Together, these findings support dissipation as a physically grounded parameter that connects enzyme kinetics, biological evolution, and nonequilibrium thermodynamics.

## Full-text entities

- **Genes:** TPI1 (triosephosphate isomerase 1) [NCBI Gene 7167] {aka HEL-S-49, TIM, TPI, TPID}, PPIC (peptidylprolyl isomerase C) [NCBI Gene 5480] {aka CYPC}, CA2 (carbonic anhydrase 2) [NCBI Gene 760] {aka CA-II, CAC, CAII, Car2, HEL-76, HEL-S-282}, EREG (epiregulin) [NCBI Gene 2069] {aka EPR, ER, Ep}, PPIA (peptidylprolyl isomerase A) [NCBI Gene 5478] {aka CYPA, CYPH, HEL-S-69p}, PCSK1 (proprotein convertase subtilisin/kexin type 1) [NCBI Gene 5122] {aka BMIQ12, NEC1, PC1, PC1/3, PC3, SPC3}, PPIB (peptidylprolyl isomerase B) [NCBI Gene 5479] {aka CYP-S1, CYPB, HEL-S-39, OI9, SCYLP}, GLB1 (galactosidase beta 1) [NCBI Gene 2720] {aka EBP, ELNR1, MPS4B}
- **Diseases:** injury to (MESH:D014947)
- **Chemicals:** chlorophyll (MESH:D002734), ADP (MESH:D000244), carbon (MESH:D002244), ATP (MESH:D000255), NADH (MESH:D009243), H+ (MESH:D006859), proton (MESH:D011522), K+ (MESH:D011188), Na+ (MESH:D012964), MPEP (-), S (MESH:D013455), Cl- (MESH:D002713)
- **Species:** Halobacterium salinarum (species) [taxon 2242], Cereibacter sphaeroides (species) [taxon 1063], Bacillus cereus (species) [taxon 1396], Escherichia coli (E. coli, species) [taxon 562], Saccharomyces cerevisiae (baker's yeast, species) [taxon 4932], Eubacterium (genus) [taxon 1730], Homo sapiens (human, species) [taxon 9606]
- **Mutations:** K29A, P99A, R25A, R214A, Y221A, R215K, Q86A, K106A

## Full text

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## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC12940570/full.md

## References

202 references — full list in the complete paper: https://tomesphere.com/paper/PMC12940570/full.md

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Source: https://tomesphere.com/paper/PMC12940570