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1Repair Windows errors before they cause bigger problems2Scan for outdated or missing drivers - takes under a minute3Clear out junk files and repair common Windows errorsPlant enzymes can favor one of two mirror-image forms of a molecule through a combination of small evolutionary changes—not just a single change at the reaction site. A study of borneol dehydrogenases reconstructed ancestral enzymes and found that changes in distant parts of the proteins helped tune how long each form stayed in a position suited to react.
What are mirror-image molecules?
Some molecules come in two forms that have the same atoms connected in the same order but are arranged as mirror images. These are called enantiomers. Like a left hand and a right hand, they are mirror images that cannot be perfectly superimposed.
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That distinction matters in biology because enzymes are themselves three-dimensional structures. A molecule that fits and reacts well in one orientation may fit less productively in its mirror-image form. Enzyme selectivity is a preference, not necessarily an absolute refusal to react with the other form.
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How did the researchers trace selectivity’s evolution?
Researchers from Freie Universität Berlin, Graz University of Technology, and Georgia Institute of Technology studied plant borneol dehydrogenases, which catalyze the conversion of borneol into camphor. Rather than observe enzyme evolution directly, the team used ancestral sequence reconstruction: they inferred likely ancestral protein sequences from a family tree of 97 plant sequences, produced reconstructed enzymes in the laboratory, and compared their behavior.
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In the university’s account of the study, the oldest unselective reconstructed enzyme, N30, was compared with the younger, highly selective N32. The two differed at 19 amino-acid positions, and only one of those changes was in the active site—the region where the reaction takes place.
Did one mutation make the enzyme selective?
No. The active-site substitution mattered, but it was not enough to produce high selectivity by itself. Introducing it into the unselective ancestor doubled selectivity; reversing it in the selective ancestor removed the enzyme’s preference. Yet high selectivity required that change together with three additional mutations located outside the active site.
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This result points to a network of changes: the reaction center contributes, but changes elsewhere in the protein help determine how effectively the enzyme favors one borneol form.
Why can mutations far from the active site matter?
The university summary reports no obvious structural differences between the reconstructed enzymes that explained their different preferences. Instead, computational simulations suggested a difference in molecular dynamics: the favored borneol form remained in a catalytically productive position longer, while the other form was held less tightly and exposed more to surrounding water.
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That is the authors’ simulation-supported interpretation, not a direct visual record of every molecular event. It offers a way to understand how mutations outside the active site could influence the bound molecule: changes elsewhere may subtly alter the enzyme’s motions and the conditions around its reaction center.
How does this compare with another plant-enzyme example?
A separate 2013 study of thyme enzymes found that two related sabinene hydrate synthases, TPS6 and TPS7, formed opposing enantiomers among similar sets of products. In that case, stereospecificity was traced to the formation of the first reaction intermediate, and one amino-acid position had a major effect.
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The thyme example is a different enzyme family and reaction, not part of the borneol-dehydrogenase study. Together, the examples show that plants can arrive at stereochemical differences through distinct routes: the borneol work points to a combination of active-site and peripheral changes affecting dynamics, while the thyme study identified an important role for an early reaction step and a particular amino-acid position.
Could this help make medicines or fragrances?
The researchers suggest that enzyme engineering may need to look beyond the active site when trying to tune selectivity. Borneol and its mirror-image form, isoborneol, can be obtained as a mixture from α-pinene, which the university summary describes as an inexpensive bio-based raw material. More selective enzymes could potentially help produce or separate individual forms for pharmaceutical, cosmetic, and fragrance uses.
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Those are possible future applications, not evidence of a commercial process or established industrial deployment. The study’s broader practical implication is that distant protein regions may offer useful targets when designing enzymes for a preferred reaction outcome.
What the study establishes—and what it does not
The 2026 study, “Deciphering the Evolutionary Origin of the Enantioselectivity of Short-Chain Dehydrogenases from Plants Toward 1-Borneol,” was summarized by Freie Universität Berlin on October 1, 2026. The summary describes reconstructed ancestral enzymes, mutation tests, and simulations; it does not establish that every enzyme distinguishes enantiomers in the same way.
As coauthor and Freie Universität Berlin researcher Dr. Bernhard Loll put it: “We were able to demonstrate how the different reaction to the two different borneol forms developed over the course of the enzymes’ evolution. What was crucial here was not major structural changes to the enzyme, but the interplay of many small changes that influenced the dynamics of the enzyme and bound molecule. This provides us with important indications of how enzymes could be specifically engineered for biotechnological applications in the future.”
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