NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor

To develop a nicotinamide-independent single flavoenzyme system for the asymmetric bioreduction of C=C bonds, four types of hydrogen donor, encompassing more than 50 candidates, were investigated. Six highly potent, cheap, and commercially available co-substrates were identified that (under the opti...

Descripción completa

Detalles Bibliográficos
Autores principales: Winkler, Christoph K, Clay, Dorina, Entner, Marcello, Plank, Markus, Faber, Kurt
Formato: Online Artículo Texto
Lenguaje:English
Publicado: WILEY-VCH Verlag 2014
Materias:
Full Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4413776/
https://www.ncbi.nlm.nih.gov/pubmed/24382795
http://dx.doi.org/10.1002/chem.201303897
_version_ 1782368831494160384
author Winkler, Christoph K
Clay, Dorina
Entner, Marcello
Plank, Markus
Faber, Kurt
author_facet Winkler, Christoph K
Clay, Dorina
Entner, Marcello
Plank, Markus
Faber, Kurt
author_sort Winkler, Christoph K
collection PubMed
description To develop a nicotinamide-independent single flavoenzyme system for the asymmetric bioreduction of C=C bonds, four types of hydrogen donor, encompassing more than 50 candidates, were investigated. Six highly potent, cheap, and commercially available co-substrates were identified that (under the optimized conditions) resulted in conversions and enantioselectivities comparable with, or even superior to, those obtained with traditional two-enzyme nicotinamide adenine dinucleotide phosphate (NAD(P)H)-recycling systems.
format Online
Article
Text
id pubmed-4413776
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher WILEY-VCH Verlag
record_format MEDLINE/PubMed
spelling pubmed-44137762015-05-05 NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor Winkler, Christoph K Clay, Dorina Entner, Marcello Plank, Markus Faber, Kurt Chemistry Full Papers To develop a nicotinamide-independent single flavoenzyme system for the asymmetric bioreduction of C=C bonds, four types of hydrogen donor, encompassing more than 50 candidates, were investigated. Six highly potent, cheap, and commercially available co-substrates were identified that (under the optimized conditions) resulted in conversions and enantioselectivities comparable with, or even superior to, those obtained with traditional two-enzyme nicotinamide adenine dinucleotide phosphate (NAD(P)H)-recycling systems. WILEY-VCH Verlag 2014-01-27 2013-12-30 /pmc/articles/PMC4413776/ /pubmed/24382795 http://dx.doi.org/10.1002/chem.201303897 Text en © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Full Papers
Winkler, Christoph K
Clay, Dorina
Entner, Marcello
Plank, Markus
Faber, Kurt
NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor
title NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor
title_full NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor
title_fullStr NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor
title_full_unstemmed NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor
title_short NAD(P)H-Independent Asymmetric C=C Bond Reduction Catalyzed by Ene Reductases by Using Artificial Co-substrates as the Hydrogen Donor
title_sort nad(p)h-independent asymmetric c=c bond reduction catalyzed by ene reductases by using artificial co-substrates as the hydrogen donor
topic Full Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4413776/
https://www.ncbi.nlm.nih.gov/pubmed/24382795
http://dx.doi.org/10.1002/chem.201303897
work_keys_str_mv AT winklerchristophk nadphindependentasymmetricccbondreductioncatalyzedbyenereductasesbyusingartificialcosubstratesasthehydrogendonor
AT claydorina nadphindependentasymmetricccbondreductioncatalyzedbyenereductasesbyusingartificialcosubstratesasthehydrogendonor
AT entnermarcello nadphindependentasymmetricccbondreductioncatalyzedbyenereductasesbyusingartificialcosubstratesasthehydrogendonor
AT plankmarkus nadphindependentasymmetricccbondreductioncatalyzedbyenereductasesbyusingartificialcosubstratesasthehydrogendonor
AT faberkurt nadphindependentasymmetricccbondreductioncatalyzedbyenereductasesbyusingartificialcosubstratesasthehydrogendonor

Ejemplares similares