Stanford researchers have uncovered how enzymes dramatically accelerate biochemical reactions, shedding light on one of life’s great mysteries. Using over 1,000 X-ray snapshots, they have quantified the chemical and physical interactions responsible for enzymes extraordinary reaction rates. Their findings could impact fields ranging from basic science to drug discovery and challenge conventional teaching methods in biochemistry.  

Dan Herschlag, professor of biochemistry at Stanford, explained that enzymes can speed up reactions by a trillion-trillion times, yet a precise understanding of how they achieve this has remained elusive. Previous models have described enzyme function in words rather than quantitatively, leading to debate among biochemists. The new research focuses on how enzymes exist in dynamic states, constantly shifting between different conformations during catalysis.  

Doctoral student Siyuan Du and Herschlag studied serine proteases, a well-known enzyme family, to break down enzyme catalysis into individual energetic contributions at the active site. They discovered that enzymes function through a combination of positioning reacting molecules and applying subtle forces that push reactions forward, much like a coiled spring releasing energy. Their findings show that nature has evolved these catalytic mechanisms independently across different enzyme families, suggesting the potential to replicate these strategies in enzyme design.  

By translating enzyme function into simple chemical principles, this research could revolutionize biochemistry education and enable the creation of more efficient, tailored enzymes for industrial and medical applications. Understanding enzymes at this fundamental level brings science closer to engineering enzymes with precision, opening new possibilities in biotechnology.

Source: https://news.stanford.edu/stories/2025/02/quantitative-comparisons-of-enzymes-in-action-could-reshape-biochemistry