ArticleNature communications2023
Thermodynamic principle to enhance enzymatic activity using the substrate affinity.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.ACS catalysis · 2025Article
- Improvement in lignin peroxidase oxidative stability via surface display by Bacillus subtilis.Biotechnology letters · 2025Article
- The Sabatier principle governs the performance of self-sufficient heterogeneous biocatalysts for redox biotransformations.Cell reports. Physical science · 2025Article
- Linking Cell Size, VEnvironmental microbiology reports · 2025Article
- Synergistic cell-free enzyme cocktails for enhanced fiber matrix development: improving dewatering, strength, and decarbonization in the paper industry.Biotechnology for biofuels and bioproducts · 2025Article
- Thermodynamics Underpinning the Microbial Community-Level Nitrogen Energy Metabolism.Environmental microbiology · 2025Article
- Article
- Free-energy transduction mechanisms shape the flux space of metabolic networks.Biophysical journal · 2024Article
- Bioreceptor modified electrochemical biosensors for the detection of life threating pathogenic bacteria: a review.RSC advances · 2024Review
- Directed-evolution mutations enhance DNA-binding affinity and protein stability of the adenine base editor ABE8e.Cellular and molecular life sciences : CMLS · 2024Article
- Revealing isochoric water nucleation: a visual study.Scientific reports · 2024Article
- Bioluminescence of (International journal of molecular sciences · 2024Article
- Thermodynamic principle to enhance enzymatic activity using the substrate affinity.Nature communications · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding how to tune enzymatic activity is important not only for biotechnological applications, but also to elucidate the basic principles guiding the design and optimization of biological systems in nature. So far, the Michaelis-Menten equation has provided a fundamental framework of enzymatic activity. However, there is still no concrete guideline on how the parameters should be optimized towards higher activity. Here, we demonstrate that tuning the Michaelis-Menten constant ([Formula: see text]) to the substrate concentration ([Formula: see text]) enhances enzymatic activity. This guideline ([Formula: see text]) was obtained mathematically by assuming that thermodynamically favorable reactions have higher rate constants, and that the total driving force is fixed. Due to the generality of these thermodynamic considerations, we propose [Formula: see text] as a general concept to enhance enzymatic activity. Our bioinformatic analysis reveals that the [Formula: see text] and in vivo substrate concentrations are consistent across a dataset of approximately 1000 enzymes, suggesting that even natural selection follows the principle [Formula: see text].
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