Discovery of factors to improve enzyme activity

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February 29, 2024

Towards the development of active enzymes and understanding the origins of enzyme diversity

A research group of RIKEN CSRS verified the importance of the affinity between enzymes and substrates as a factor that determines enzyme activity, which has been attracting attention in recent years. The group also discovered that there are important factors such as the Arrhenius prefactor, which are as important as substrate binding affinity.

Enzymes are catalysts in living organisms and have the function of accelerating specific chemical reactions. The level of the reaction rate accelerated by the enzyme is called enzyme activity. Identifying the factors that determine enzyme activity is important not only for basic science, such as understanding biological evolution, but also for bioengineering because it may lead to the design of highly active enzymes.

In this study, the research group evaluated the factors which determine enzyme activity by experimentally measuring the activity of various phosphoserine phosphatases, and then analyzing them using the theory of catalysis. The results confirmed the importance of substrate binding affinity, which has recently attracted attention as an important factor determining enzyme activity. Additionally, the results also revealed that there are other factors, such as the Arrhenius prefactors, which can have a similar level of influence. This research suggests that it is possible to improve enzyme activity by optimizing these factors, which is expected to contribute to the development of high-performance enzymes.

Original article: Angewandte Chemie International Edition doi: 10.1002/anie.202318635; Y. Chiba, H. Ooka, M. E. Wintzer, N. Tsunematsu, T. Nogawa, T. Suzuki, N. Dohmae, R. Nakamura,; "Rationalizing the Influence of the Binding Affinity on the Activity of Phosphoserine Phosphatases".
Contact: Yoko Chiba; Senior Scientist
Hideshi Ooka; Research Scientist
Ryuhei Nakamura; Team Leader
Team Leader
Biofunctional Catalyst Research Team