Division of Chemistry and Biochemistry, Graduate School of Natural Science and Technology, Okayama University, Tsushima, Okayama 700-8530, Japan.
Chem Commun (Camb). 2010 Aug 14;46(30):5440-2. doi: 10.1039/c001561j. Epub 2010 Apr 9.
Catalytic activity and enantioselectivity of lipase toward poor substrates bearing bulky substituents on both sides have been dramatically improved by rational design; the E value for a poor substrate was increased from 5 (wild-type enzyme) to >200 (I287F/I290A double mutant) with an acceleration of the reaction rate.
通过合理设计，极大地提高了脂肪酶对两侧带有大取代基的不良底物的催化活性和对映选择性；与野生型酶相比，E 值对不良底物的提高了 5 倍（野生型酶）至 >200 倍（I287F/I290A 双突变体），反应速率也得到了加速。
