Reetz Manfred T, Torre Claudia, Eipper Andreas, Lohmer Renate, Hermes Marcus, Brunner Birgit, Maichele Andrea, Bocola Marco, Arand Michael, Cronin Annette, Genzel Yvonne, Archelas Alain, Furstoss Roland
Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim/Ruhr, Germany, Institut für Pharmakologie und Toxikologie, Universität Würzburg, Versbacher Strasse 9, 97078 Würzburg, Germany.
Org Lett. 2004 Jan 22;6(2):177-80. doi: 10.1021/ol035898m.
[reaction: see text] The epoxide hydrolase (EH) from Aspergillus niger, which shows a selectivity factor of only E = 4.6 in the hydrolytic kinetic resolution of glycidyl phenyl ether, has been subjected to directed evolution for the purpose of enhancing enantioselectivity. After only one round of error-prone polymerase chain reaction (epPCR), enantioselectivity was more than doubled (E = 10.8). The improved mutant enzyme contains three amino acid exchanges, two of which are spatially far from the catalytically active center.
[反应：见正文] 黑曲霉的环氧水解酶（EH）在缩水甘油基苯基醚的水解动力学拆分中显示出仅E = 4.6的选择性因子，为提高对映选择性而进行了定向进化。仅经过一轮易错聚合酶链反应（epPCR）后，对映选择性就增加了一倍多（E = 10.8）。改进的突变酶包含三个氨基酸交换，其中两个在空间上远离催化活性中心。
