In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase

An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer–Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis. Several substrates composed of different s...

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Detalles Bibliográficos
Autores principales: Oberleitner, Nikolin, Peters, Christin, Rudroff, Florian, Bornscheuer, Uwe T., Mihovilovic, Marko D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science Publishers 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263279/
https://www.ncbi.nlm.nih.gov/pubmed/24746588
http://dx.doi.org/10.1016/j.jbiotec.2014.04.008
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author Oberleitner, Nikolin
Peters, Christin
Rudroff, Florian
Bornscheuer, Uwe T.
Mihovilovic, Marko D.
author_facet Oberleitner, Nikolin
Peters, Christin
Rudroff, Florian
Bornscheuer, Uwe T.
Mihovilovic, Marko D.
author_sort Oberleitner, Nikolin
collection PubMed
description An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer–Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis. Several substrates composed of different structural motifs were examined and provided access to functionalized chiral compounds in high yields (up to >99%) and optical purities (up to >99%). Hence, the applicability of the presented enzymatic cascade was exploited for the synthesis of biorenewable polyesters.
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spelling pubmed-42632792014-12-20 In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase Oberleitner, Nikolin Peters, Christin Rudroff, Florian Bornscheuer, Uwe T. Mihovilovic, Marko D. J Biotechnol Article An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer–Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis. Several substrates composed of different structural motifs were examined and provided access to functionalized chiral compounds in high yields (up to >99%) and optical purities (up to >99%). Hence, the applicability of the presented enzymatic cascade was exploited for the synthesis of biorenewable polyesters. Elsevier Science Publishers 2014-12-20 /pmc/articles/PMC4263279/ /pubmed/24746588 http://dx.doi.org/10.1016/j.jbiotec.2014.04.008 Text en © 2014 The Authors https://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Article
Oberleitner, Nikolin
Peters, Christin
Rudroff, Florian
Bornscheuer, Uwe T.
Mihovilovic, Marko D.
In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
title In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
title_full In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
title_fullStr In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
title_full_unstemmed In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
title_short In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
title_sort in vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a baeyer–villiger monooxygenase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263279/
https://www.ncbi.nlm.nih.gov/pubmed/24746588
http://dx.doi.org/10.1016/j.jbiotec.2014.04.008
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