Researchers Mapped Evolution of Enzyme Selectivity
The study reveals how plant enzymes evolved to distinguish between mirror-image molecular structures.
Updated on Oct. 9, 2026 in Life Sciences
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Researchers have reconstructed the evolutionary history of plant enzymes known as borneol dehydrogenases to understand how they evolved to differentiate between mirror-image molecules. This research, which is currently in the scientific study stage, identified the specific mutations responsible for this precise selectivity.
Why it matters
Understanding the evolution of enzyme precision enables more effective protein engineering for pharmaceutical and chemical production. By identifying how peripheral mutations influence active sites, scientists can better design biocatalysts for complex molecular synthesis.
The team analyzed 97 plant sequences to identify how 19 amino acid mutations evolved to refine enzyme selectivity. Computational simulations demonstrated that selectivity hinges on the duration a substrate molecule maintains a productive position within the catalytic site.
The players
Freie Universität Berlin
A German public research university that focuses on advanced chemical and biological sciences.
Graz University of Technology
An Austrian technical university with expertise in biotechnology and process engineering.
Georgia Institute of Technology
A U.S.-based research institution known for its programs in bioengineering and synthetic biology.
The details
Researchers used ancestral sequence reconstruction—a computational method that uses evolutionary data to infer and synthesize extinct protein forms—to study the shift from non-selective to selective enzyme function. They focused on borneol dehydrogenases, which convert the compound borneol into camphor. The process revealed that mutations far from the enzyme’s active site—the specific pocket where chemical reactions occur—can reconfigure the enzyme’s geometry to favor one mirror-image molecule over another.
Timeline
October 9, 2026: Study published in Nature Communications.
The Tech Race
This work follows the broader trend of using ancestral sequence reconstruction to map the origins of biological function. It provides a new architectural framework for enzyme engineering that competes with traditional trial-and-error directed evolution methods.
This research provides a foundational blueprint for scientists to engineer more efficient enzymes for pharmaceutical synthesis. Future applications will depend on successful laboratory validation of these computationally predicted mutations in commercial production workflows.
The takeaway
The study demonstrates that enzyme precision is governed by specific mutations located far from the active site, suggesting a new target for protein engineers. Watch for subsequent papers demonstrating the implementation of these mutations in industrial biocatalysis to confirm the scalability of this method.
Further reading
Explore more developments in protein engineering in Life Sciences.
More information
View the complete findings in the Nature Communications research article.
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