Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates
Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates
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DOI：
10.1039/c001561j
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发表时间：
2010-01-01
影响因子：
4.9
通讯作者：
Sakai, Takashi
中科院分区：
文献类型：
--
作者：
Ema, Tadashi;Kamata, Shusuke;Sakai, Takashi
通过合理设计，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得到了显著提高，对不良底物的E值从5（野生型酶）提高到>200（I287 F/I290 A双突变体），反应速率加快。
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.