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Kinetic Resolution of Racemic Primary Amines Using Geobacillus stearothermophilus Amine Dehydrogenase Variant
Author(s) -
Tseliou Vasilis,
Knaus Tanja,
Vilím Jan,
Masman Marcelo F.,
Mutti Francesco G.
Publication year - 2020
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201902085
Subject(s) - geobacillus stearothermophilus , kinetic resolution , chemistry , amine gas treating , formate dehydrogenase , yield (engineering) , primary (astronomy) , kinetics , dehydrogenase , enzyme , stereochemistry , organic chemistry , combinatorial chemistry , cofactor , catalysis , materials science , thermophile , enantioselective synthesis , physics , astronomy , quantum mechanics , metallurgy
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 .