ArticleChemistryOpen2022
Computational Study of Mechanism and Enantioselectivity of Imine Reductase from Amycolatopsis orientalis.
Article in ChemistryOpen, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Activity and Enantioselectivity of Hydroxynitrile Lyase from Granulicella tundricula: Computational Insights.Inorganic chemistry · 2026Article
- Physics-based modeling in the new era of enzyme engineering.Nature computational science · 2025Review
- A Quantum Mechanical Approach to The Mechanism of Asymmetric Synthesis of Chiral Amine by Imine Reductase from Stackebrandtia Nassauensis.ChemPlusChem · 2025Article
- Deciphering the Unconventional Reduction of C=N Bonds by Old Yellow Enzymes Using QM/MM.ACS catalysis · 2024Article
- Computational design of an imine reductase: mechanism-guided stereoselectivity reversion and interface stabilization.Chemical science · 2024Article
- The Quantum Chemical Cluster Approach in Biocatalysis.Accounts of chemical research · 2023Review
- Computational Study of Mechanism and Enantioselectivity of Imine Reductase from Amycolatopsis orientalis.ChemistryOpen · 2022Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Imine reductases (IREDs) are NADPH-dependent enzymes (NADPH=nicotinamide adenine dinucleotide phosphate) that catalyze the reduction of imines to amines. They exhibit high enantioselectivity for a broad range of substrates, making them of interest for biocatalytic applications. In this work, we have employed density functional theory (DFT) calculations to elucidate the reaction mechanism and the origins of enantioselectivity of IRED from Amycolatopsis orientalis. Two substrates are considered, namely 1-methyl-3,4-dihydroisoquinoline and 2-propyl-piperideine. A model of the active site is built on the basis of the available crystal structure. For both substrates, different binding modes are first evaluated, followed by calculation of the hydride transfer transition states from each complex. We have also investigated the effect of mutations of certain important active site residues (Tyr179Ala and Asn241Ala) on the enantioselectivity. The calculated energies are consistent with the experimental observations and the analysis of transition states geometries provides insights into the origins of enantioselectivity of this enzyme.
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