Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant

A NADH‐dependent engineered amine dehydrogenase from Geobacillus stearothermophilus (LE‐AmDH‐v1) was applied together with a NADH‐oxidase from Streptococcus mutans (NOx) for the kinetic resolution of pharmaceutically relevant racemic α‐chiral primary amines. The reaction conditions (e. g., pH, tempe...

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Autores principales: Tseliou, Vasilis, Knaus, Tanja, Vilím, Jan, Masman, Marcelo F., Mutti, Francesco G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7422701/
https://www.ncbi.nlm.nih.gov/pubmed/32802214
http://dx.doi.org/10.1002/cctc.201902085
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author Tseliou, Vasilis
Knaus, Tanja
Vilím, Jan
Masman, Marcelo F.
Mutti, Francesco G.
author_facet Tseliou, Vasilis
Knaus, Tanja
Vilím, Jan
Masman, Marcelo F.
Mutti, Francesco G.
author_sort Tseliou, Vasilis
collection PubMed
description A NADH‐dependent engineered amine dehydrogenase from Geobacillus stearothermophilus (LE‐AmDH‐v1) was applied together with a NADH‐oxidase from Streptococcus mutans (NOx) for the kinetic resolution of pharmaceutically relevant racemic α‐chiral primary amines. The reaction conditions (e. g., pH, temperature, type of buffer) were optimised to yield S‐configured amines with up to >99 % ee.
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spelling pubmed-74227012020-08-13 Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant Tseliou, Vasilis Knaus, Tanja Vilím, Jan Masman, Marcelo F. Mutti, Francesco G. ChemCatChem Communications A NADH‐dependent engineered amine dehydrogenase from Geobacillus stearothermophilus (LE‐AmDH‐v1) was applied together with a NADH‐oxidase from Streptococcus mutans (NOx) for the kinetic resolution of pharmaceutically relevant racemic α‐chiral primary amines. The reaction conditions (e. g., pH, temperature, type of buffer) were optimised to yield S‐configured amines with up to >99 % ee. John Wiley and Sons Inc. 2020-03-06 2020-04-20 /pmc/articles/PMC7422701/ /pubmed/32802214 http://dx.doi.org/10.1002/cctc.201902085 Text en © 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Communications
Tseliou, Vasilis
Knaus, Tanja
Vilím, Jan
Masman, Marcelo F.
Mutti, Francesco G.
Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
title Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
title_full Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
title_fullStr Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
title_full_unstemmed Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
title_short Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
title_sort kinetic resolution of racemic primary amines using geobacillus stearothermophilus amine dehydrogenase variant
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7422701/
https://www.ncbi.nlm.nih.gov/pubmed/32802214
http://dx.doi.org/10.1002/cctc.201902085
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