Enantioselective Switch and Potential Applications in Biocatalysis

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 condi-tions. A transaminase from Halomonas elongata (& omega;-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 en-zymes are reported to have a similar behavior, and here we discuss some of them and their potential applications.

Automated summary

Enzymatic synthesis always involves enantioselectivity, and it is possible to induce a switch in enantioselectivity by adjusting reaction conditions. For instance, the transaminase from Halomonas elongata (& omega;-HeWT) can shift from generating the S-enantiomer to the R-enantiomer at higher concentrations of amino acceptor or ionic strength. Similar behavior has been observed in other enzymes, and this article discusses some of them and their potential applications.