5OJL

Imine Reductase from Aspergillus terreus in complex with NADPH4 and dibenz[c,e]azepine

Summary for 5OJL

• Entry DOI: 10.2210/pdb5ojl/pdb
• Descriptor: Imine reductase, 5-methyl-7~{H}-benzo[d][2]benzazepine, 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: nadph, imine reductase, reductive aminase, oxidoreductase
• Biological source: Aspergillus terreus
• Total number of polymer chains: 1
• Total formula weight: 31710.79

Authors

Sharma, M.,Grogan, G. (deposition date: 2017-07-21, release date: 2018-05-30, Last modification date: 2024-01-17)

Primary citation

France, S.P.,Aleku, G.A.,Sharma, M.,Mangas-Sanchez, J.,Howard, R.M.,Steflik, J.,Kumar, R.,Adams, R.W.,Slabu, I.,Crook, R.,Grogan, G.,Wallace, T.W.,Turner, N.J.
Biocatalytic Routes to Enantiomerically Enriched Dibenz[c,e]azepines.
Angew. Chem. Int. Ed. Engl., 56:15589-15593, 2017

PubMed Abstract: Biocatalytic retrosynthetic analysis of dibenz[c,e]azepines has highlighted the use of imine reductase (IRED) and ω-transaminase (ω-TA) biocatalysts to establish the key stereocentres of these molecules. Several enantiocomplementary IREDs were identified for the synthesis of (R)- and (S)-5-methyl-6,7-dihydro-5H-dibenz[c,e]azepine with excellent enantioselectivity, by reduction of the parent imines. Crystallographic evidence suggests that IREDs may be able to bind one conformer of the imine substrate such that, upon reduction, the major product conformer is generated directly. ω-TA biocatalysts were also successfully employed for the production of enantiopure 1-(2-bromophenyl)ethan-1-amine, thus enabling an orthogonal route for the installation of chirality into dibenz[c,e]azepine framework.

PubMed: 29024400
DOI: 10.1002/anie.201708453

Experimental method

X-RAY DIFFRACTION (1.56 Å)