This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Many naturally occurring molecules such as menthol or limonene exist in two mirror-image forms, known as enantiomers, that look almost identical but can differ greatly in smell, taste or effect on the body. Enzymes can often distinguish between them with remarkable precision, which is why they are so valuable for the chemical and pharmaceutical industries.
How this precision evolved naturally has remained largely unknown. A team led by researchers from Freie Universität Berlin, Graz University of Technology and Georgia Institute of Technology has now reconstructed one such evolutionary path. The study, titled "Deciphering the Evolutionary Origin of the Enantioselectivity of Short-Chain Dehydrogenases from Plants Toward 1-Borneol," is published in Nature Communications.
Enzymes are biological catalysts—typically proteins—that accelerate chemical reactions. Their structure determines which molecules bind to them as well as the speed of biochemical reactions. This makes enzymes particularly valuable in biotechnology, as their properties can be harnessed to carry out specific chemical reactions.
The international research team led by Dr. Bernhard Loll from the Department of Biology, Chemistry, Pharmacy at Freie Universität Berlin, Professor Robert Kourist from Graz University of Technology, Austria, and Professor Lynn Kamerlin from Georgia Institute of Technology, United States, studied a group of plant enzymes called borneol dehydrogenases. These convert the alcohol borneol into camphor in a chemical reaction.
Borneol exists in two mirror-image forms called enantiomers that are comparable to a left hand and a right hand. Some enzymes strongly prefer the formation of one form over the other, while others barely distinguish between borneol and isoborneol. "We were able to demonstrate how the different reactions 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," explains Loll from Freie Universität Berlin, one of the authors of the study. The researchers wanted to find out how this difference emerged as these enzymes evolved.
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