Enzymatic strategies for asymmetric synthesis.
Autor: | Hall M; Institute of Chemistry, University of Graz Heinrichstrasse 28 8010 Graz Austria melanie.hall@uni-graz.at.; Field of Excellence BioHealth - University of Graz Austria. |
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Jazyk: | angličtina |
Zdroj: | RSC chemical biology [RSC Chem Biol] 2021 Jun 01; Vol. 2 (4), pp. 958-989. Date of Electronic Publication: 2021 Jun 01 (Print Publication: 2021). |
DOI: | 10.1039/d1cb00080b |
Abstrakt: | Enzymes, at the turn of the 21st century, are gaining a momentum. Especially in the field of synthetic organic chemistry, a broad variety of biocatalysts are being applied in an increasing number of processes running at up to industrial scale. In addition to the advantages of employing enzymes under environmentally friendly reaction conditions, synthetic chemists are recognizing the value of enzymes connected to the exquisite selectivity of these natural (or engineered) catalysts. The use of hydrolases in enantioselective protocols paved the way to the application of enzymes in asymmetric synthesis, in particular in the context of biocatalytic (dynamic) kinetic resolutions. After two decades of impressive development, the field is now mature to propose a panel of catalytically diverse enzymes for (i) stereoselective reactions with prochiral compounds, such as double bond reduction and bond forming reactions, (ii) formal enantioselective replacement of one of two enantiotopic groups of prochiral substrates, as well as (iii) atroposelective reactions with noncentrally chiral compounds. In this review, the major enzymatic strategies broadly applicable in the asymmetric synthesis of optically pure chiral compounds are presented, with a focus on the reactions developed within the past decade. Competing Interests: There are no conflicts to declare. (This journal is © The Royal Society of Chemistry.) |
Databáze: | MEDLINE |
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