Kinetic Resolution of Racemic Primary Amines Using <i>Geobacillus stearothermophilus</i> Amine Dehydrogenase Variant
Vasilis Tseliou, Tanja Knaus, Jan Vilím, Marcelo F. Masman, Francesco G. Mutti
Abstract
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 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 .
Topics & Concepts
Geobacillus stearothermophilusKinetic resolutionChemistryAmine gas treatingFormate dehydrogenaseYield (engineering)Primary (astronomy)KineticsDehydrogenaseEnzymeStereochemistryOrganic chemistryCombinatorial chemistryCofactorCatalysisMaterials scienceThermophileEnantioselective synthesisQuantum mechanicsMetallurgyPhysicsAstronomyEnzyme Catalysis and ImmobilizationAmino Acid Enzymes and Metabolism