This review summarized NAD(P)H-dependent amine dehydrogenases and imine reductases which catalyzes asymmetric reductive amination to produce optically active amines.
The stereoselectivity and thermal stability of imine reductase are manipulated through computational design, based on predicted catalytic mechanisms and subunit interfaces.
Multiple residues have been identified at the cofactor and substrate binding pockets in a reductive aminase that can be exploited for stereocontrol through steric modification of their side chains.
Chiral 1-substituted-THβC can be synthesized from L-tryptophan or tryptamine by Pictet–Spengler reaction and chiral auxiliary; also from substituted-DHβC by ATH reaction with chiral catalysts, asymmetric addition reaction, and enzymatic catalysis.
A highly efficient biocatalytic dynamic kinetic resolution (DKR) for the asymmetric synthesis of axially chiral heterobiaryls and heterobiaryl N-oxides was developed using engineered imine-reductases (IREDs).