Semisynthetic enzymes in asymmetric synthesis:: Enantioselective reduction of racemic hydroperoxides catalyzed by seleno-subtilisin
Semisynthetic enzymes in asymmetric synthesis:: Enantioselective reduction of racemic hydroperoxides catalyzed by seleno-subtilisin
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DOI：
10.1021/jo981665a
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发表时间：
1999-02-05
影响因子：
3.6
通讯作者：
Schreier, P
中科院分区：
文献类型：
--
作者：
Häring, D;Schüler, E;Schreier, P
丝氨酸蛋白酶枯草杆菌蛋白酶被化学转化为过氧化物酶活性的硒枯草杆菌蛋白酶。这种半合成酶催化外消旋氢过氧化物在硫酚存在下的对映选择性还原，以产生光学活性的氢过氧化物和醇的半制备规模。测定了硒代枯草杆菌蛋白酶催化还原各种手性氢过氧化物的动力学参数和对映选择性。这种半合成酶的催化效率与天然辣根过氧化物酶的催化效率相当。硒代枯草杆菌蛋白酶的对映体选择性的意义与以前用于合成光学活性氢过氧化物的天然酶相反。因此，半合成酶硒枯草杆菌蛋白酶补充了天然可用的过氧化物酶的不对称合成两种对映体。
The serine protease subtilisin was chemically converted into the peroxidase-active seleno-subtilisin. This semisynthetic enzyme catalyzes the enantioselective reduction of racemic hydroperoxides in the presence of thiophenols to yield optically active hydroperoxides and alcohols on the semipreparative scale. The kinetic parameters and enantioselectivities of seleno-subtilisin-catalyzed reduction of various chiral hydroperoxides were determined. The catalytic efficiency of this semisynthetic enzyme is comparable to that of the native horseradish peroxidase. The sense in the enantioselectivity of the seleno-subtilisin is opposite to the natural enzymes previously used in the synthesis of optically active hydroperoxides. Consequently, the semisynthetic enzyme selenosubtilisin complements the naturally available peroxidases for the asymmetric synthesis of both enantiomers.