Abstract
Enantioselectivity has always been a key feature of enzymatic synthesis. In some cases, when enzymes are not strictly enantioselective, it is possible to induce an enantioselective switch by tuning the reaction conditions. A transaminase from Halomonas elongata (ω-HeWT), while generally S-selective, could be shifted towards generating the R-enantiomer at higher concentrations of amino acceptor or ionic strength, for example. Other enzymes are reported to have a similar behavior, and here we discuss some of them and their potential applications.
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Robustini, L., & Paradisi, F. (2023). Enantioselective Switch and Potential Applications in Biocatalysis. Chimia, 77(6), 390–394. https://doi.org/10.2533/chimia.2023.390
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