How to enhance enzymatic reaction rates? The Sabatier principle and beyond

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Catalytic efficiency can be improved by optimizing Km without compromising kcat, leading to enhanced enzymatic activity.
Recent studies highlight the interdependence of kcat and Km in enzymatic reactions while emphasizing potential strategies to enhance them.
The review discusses breaking the trade-off between kcat and Km, allowing for improved enzymatic reaction rates in industrial applications.
Optimal Km values may vary across different enzymes, indicating the potential applicability of this concept across a wide range.

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Review summarizes advancements for optimizing catalytic activity and maximizing enzymatic efficiency by breaking Km and kcat trade-off.

Chiba et al. (2025) studied this question.

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