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


ABSTRACT: 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 ?-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.

SUBMITTER: Tseliou V 

PROVIDER: S-EPMC7422701 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

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Kinetic Resolution of Racemic Primary Amines Using <i>Geobacillus stearothermophilus</i> Amine Dehydrogenase Variant.

Tseliou Vasilis V   Knaus Tanja T   Vilím Jan J   Masman Marcelo F MF   Mutti Francesco G FG  

ChemCatChem 20200306 8


A NADH-dependent engineered amine dehydrogenase from <i>Geobacillus stearothermophilus</i> (LE-AmDH-v1) was applied together with a NADH-oxidase from <i>Streptococcus mutans</i> (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 <i>S</i>-configured amines with up to >99 % <i>ee</i>. ...[more]

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