Mutagenesis of the active‐site residues of the epoxide hydrolase StEH1 led to enzyme variants with modified enantiopreference for (2,3‐epoxypropyl)benzene. The wild‐type enzyme favors the S enantiomer, whereas a quadruple mutant displays a 15:1 preference for the R enantiomer, due to crippled catalytic efficiency in the hydrolysis of the S enantiomer, but retained activity with the R enantiomer.

中文翻译：

---

底物特异性的改变导致对映体偏向于（2,3-环氧丙丙基）苯的环氧水解酶

诱变的环氧化物的活性位点残基的水解酶StEH1导致酶与（2,3-环氧丙基）苯改性enantiopreference变体。野生型酶有利于S对映异构体，而四倍体突变体则对R对映异构体显示15：1的偏好，这是由于S对映异构体水解的催化效率降低，但保留了R对映异构体的活性。