Article
Deciphering the evolutionary origin of the enantioselectivity of short-chain dehydrogenases from plants toward 1-borneol.
Nature communications - 14 Aug 2026
Zuson Jasmin, Helmer Carl P O, Di Geronimo Bruno, Chánique Andrea M, Kavčiaková Katarína, Teijeiro-Juiz Rosa, Brickel Sebastian, Ramirez Molina Nuria, Drienovská Ivana, Kracher Daniel, Gaucher Eric A, Kamerlin Shina Caroline Lynn, Loll Bernhard, Kourist Robert
Abstract excerpt
Enzyme engineering has produced numerous methods to optimize enzymes for biotechnological processes; however, less is known about how natural evolution creates new functionalities. We investigate the evolutionary emergence of enantioselectivity in plant borneol dehydrogenases, which feature hydrophobic active-sites and are enantioselective towards dibornane-type monoterpenols. Ancestral sequence reconstruction...
Read the complete abstract on PubMedTopics
- Evolution, Molecular
- Stereoisomerism
- Catalytic Domain
- Substrate Specificity
- Short Chain Dehydrogenase-Reductases
