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Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant.
Tseliou, Vasilis; Knaus, Tanja; Vilím, Jan; Masman, Marcelo F; Mutti, Francesco G.
Afiliação
  • Tseliou V; van 't Hoff Institute for Molecular Sciences HIMS-Biocat University of Amsterdam Science Park 904 1098 XH Amsterdam (The Netherlands.
  • Knaus T; van 't Hoff Institute for Molecular Sciences HIMS-Biocat University of Amsterdam Science Park 904 1098 XH Amsterdam (The Netherlands.
  • Vilím J; van 't Hoff Institute for Molecular Sciences HIMS-Biocat University of Amsterdam Science Park 904 1098 XH Amsterdam (The Netherlands.
  • Masman MF; van 't Hoff Institute for Molecular Sciences HIMS-Biocat University of Amsterdam Science Park 904 1098 XH Amsterdam (The Netherlands.
  • Mutti FG; van 't Hoff Institute for Molecular Sciences HIMS-Biocat University of Amsterdam Science Park 904 1098 XH Amsterdam (The Netherlands.
ChemCatChem ; 12(8): 2184-2188, 2020 Apr 20.
Article em En | MEDLINE | ID: mdl-32802214
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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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: ChemCatChem Ano de publicação: 2020 Tipo de documento: Article País de publicação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: ChemCatChem Ano de publicação: 2020 Tipo de documento: Article País de publicação: Alemanha