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Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds
Ene-reductases from the ‘Old Yellow Enzyme’ family of flavoproteins catalyze the asymmetric reduction of various α,β-unsaturated compounds at the expense of a nicotinamide cofactor. They have been applied to the synthesis of valuable enantiopure products, including chiral building blocks with broad...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Science Publishers
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3521962/ https://www.ncbi.nlm.nih.gov/pubmed/22498437 http://dx.doi.org/10.1016/j.jbiotec.2012.03.023 |
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author | Winkler, Christoph K. Tasnádi, Gábor Clay, Dorina Hall, Mélanie Faber, Kurt |
author_facet | Winkler, Christoph K. Tasnádi, Gábor Clay, Dorina Hall, Mélanie Faber, Kurt |
author_sort | Winkler, Christoph K. |
collection | PubMed |
description | Ene-reductases from the ‘Old Yellow Enzyme’ family of flavoproteins catalyze the asymmetric reduction of various α,β-unsaturated compounds at the expense of a nicotinamide cofactor. They have been applied to the synthesis of valuable enantiopure products, including chiral building blocks with broad industrial applications, terpenoids, amino acid derivatives and fragrances. The combination of these highly stereoselective biocatalysts with a cofactor recycling system has allowed the development of cost-effective methods for the generation of optically active molecules, which is strengthened by the availability of stereo-complementary enzyme homologues. |
format | Online Article Text |
id | pubmed-3521962 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Elsevier Science Publishers |
record_format | MEDLINE/PubMed |
spelling | pubmed-35219622012-12-31 Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds Winkler, Christoph K. Tasnádi, Gábor Clay, Dorina Hall, Mélanie Faber, Kurt J Biotechnol Article Ene-reductases from the ‘Old Yellow Enzyme’ family of flavoproteins catalyze the asymmetric reduction of various α,β-unsaturated compounds at the expense of a nicotinamide cofactor. They have been applied to the synthesis of valuable enantiopure products, including chiral building blocks with broad industrial applications, terpenoids, amino acid derivatives and fragrances. The combination of these highly stereoselective biocatalysts with a cofactor recycling system has allowed the development of cost-effective methods for the generation of optically active molecules, which is strengthened by the availability of stereo-complementary enzyme homologues. Elsevier Science Publishers 2012-12-31 /pmc/articles/PMC3521962/ /pubmed/22498437 http://dx.doi.org/10.1016/j.jbiotec.2012.03.023 Text en © 2012 Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/3.0/Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license |
spellingShingle | Article Winkler, Christoph K. Tasnádi, Gábor Clay, Dorina Hall, Mélanie Faber, Kurt Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
title | Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
title_full | Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
title_fullStr | Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
title_full_unstemmed | Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
title_short | Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
title_sort | asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3521962/ https://www.ncbi.nlm.nih.gov/pubmed/22498437 http://dx.doi.org/10.1016/j.jbiotec.2012.03.023 |
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