Imine reductase

IREDs were originally discovered in 2010 by screening bacterial strains for reducing activity on 2-methyl-1-pyrroline (2-MPN).

[1][2] The conversion is not a genuine reductive amination as only the second half of the two-part reaction is catalyzed.

In 2017 an IRED was discovered that catalyzed both steps of reductive amination of a wide scope of ketone-amine pairs.

[1][2] Engineered RedAms have been employed in industrial processes to support production of pharmaceuticals for clinical trials and commercial manufacturing.

[3][11] Each protomer's α-helical dimerization domain wraps around the interdomain helix of its dimer partner forming the substrate-binding cleft above the NAD(P)H cofactor binding site in the Rossmann domain.