Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: Enzyme-based stereocontrol
Asymmetric bioreduction of C=C bonds using enoate reductases OPR1, OPR3 and YqjM: Enzyme-based stereocontrol
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DOI：
10.1002/adsc.200700458
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发表时间：
2008-02-01
影响因子：
5.4
通讯作者：
Faber, Kurt
中科院分区：
文献类型：
--
作者：
Hall, Melanie;Stueckler, Clemens;Faber, Kurt
研究了三种克隆的黄素蛋白“老黄酶”家族的烯酸还原酶在活性烯烃不对称还原反应中的作用。12-来自番茄（Lycopersicon esculentum）的氧代植物二烯酸还原酶同工酶OPR 1和OPR 3以及来自枯草芽孢杆菌（Bacillus subtilis）的YqjM通过还原α，β-不饱和醛、酮、马来酰亚胺和硝基烯烃而显示出非常宽的底物谱。该反应以绝对的化学选择性进行-仅共轭C=C键被还原，而分离的烯烃和羰基基团保持完整-具有优异的立体选择性（ees高达> 99%）。硝基烯烃还原后，立体化学的结果可以通过选择适当的酶（OPR 1与OPR 3或YqjM），这提供了相应的对映体硝基烷烃在优秀ee. Molecular建模表明，这种“酶为基础的立体控制”是由活性部位的几何形状内的细微差异。
Three cloned enoate, reductases from the "old yellow enzyme" family of flavoproteins were investigated in the asymmetric bioreduction of activated alkenes. 12-Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from Lycopersicon esculentum (tomato), and YqjM from Bacillus subtilis displayed a remarkably broad substrate spectrum by reducing a,p-unsaturated aldehydes, ketones, maleimides and nitroalkenes. The reaction proceeded with absolute chemoselectivity - only the conjugated C=C bond was reduced, while isolated olefins and carbonyl groups remained intact - with excellent stereoselectivities (ees up to > 99%). Upon reduction of a nitroalkene, the stereochemical outcome could be determined via choice of the appropriate enzyme (OPR1 versus OPR3 or YqjM), which furnished the corresponding enantiomeric nitroalkanes in excellent ee. Molecular modelling suggests that this "enzyme-based stereocontrol" is caused by subtle differences within the active site geometries.