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.
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).
The chirality introduced at the C1 position of 1-substituted-1,2,3,4-tetrahydroisoquinolines, obtained by four methods of enantioselective reduction of 1-substituted-3,4-dihydroisoquinolines, are vital for various biological activities.
In this study, engineered imine reductases (IREDs) of IRED M5, originally from Actinoalloteichus hymeniacidonis, were obtained through structure-guided semi-rational design.