A substrate-driven approach to determine reactivities of α,β-unsaturated carboxylic esters towards asymmetric bioreduction 机翻标题: 暂无翻译,请尝试点击翻译按钮。

来源
Chemistry: A European journal
年/卷/期
2012 / 18 / 33
页码
10362-10367
ISSN号
0947-6539
作者单位
ACIB GmbH C/o, Biocatalytic Synthesis, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;Fine Chemicals and Biocatalysis Research, BASF SE, Carl-Bosch-Strasse 38, 67056 Ludwigshafen, Germany;Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010-Graz, Austria;
作者
Tasnádi, G.;Winkler, C.K.;Clay, D.;Sultana, N.;Fabian, W.M.F.;Hall, M.;Ditrich, K.;Faber, K.;
摘要
The degree of C=C bond activation in the asymmetric bioreduction of α,β-unsaturated carboxylic esters by ene-reductases was studied, and general recommendations to render these "borderline-substrates" more reactive towards enzymatic reduction are proposed. The concept of "supported substrate activation" was developed. In general, an additional α-halogenated substituent proved to be beneficial for enzymatic activity, whereas β-alkyl or β-aryl substituents were detrimental for the reactivity of nonhalogenated substrates, and α-cyano groups showed little effect. The alcohol moiety of the ester functionality was found to have a strong influence on the reaction rate. Overall, activities were determined by both steric and electronic effects. Biotransformation: The asymmetric bioreduction of α,β-unsaturated carboxylic esters by ene-reductases could be tuned by varying the degree of C=C bond activation (see scheme). An additional α-halogenated substituent proved to be beneficial for enzymatic activity, whereas β-alkyl or β-aryl substituents were detrimental for the reactivity of nonhalogenated substrates.
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关键词/主题词
biocatalysis;ene-reductase;enzymes;substituent effects;substrate activation;
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