ArticleCommunications chemistry2022
Actinomycetes-derived imine reductases with a preference towards bulky amine substrates.
Article in Communications chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 25 citations in OpenAlex.
- Chemoenzymatic synthesis.Communications chemistry · 2025Article
- Discovery and Synthetic Applications of a NAD(P)H-Dependent Reductive Aminase fromACS catalysis · 2025Article
- Asymmetric Synthesis of 2-Arylethylamines: A Metal-Free Review of the New Millennium.Molecules (Basel, Switzerland) · 2024Review
- Biosynthesis of Diverse Ephedra-Type Alkaloids via a Newly Identified Enzymatic Cascade.Biodesign research · 2024Article
- Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.Acta crystallographica. Section F, Structural biology communications · 2023Article
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Authors and funding
17 authors at 3 institutions in 2 countries.
Funding
Abstract
Since imine reductases (IREDs) were reported to catalyze the reductive amination reactions, they became particularly attractive for producing chiral amines. Though diverse ketones and aldehydes have been proved to be excellent substrates of IREDs, bulky amines have been rarely transformed. Here we report the usage of an Increasing-Molecule-Volume-Screening to identify a group of IREDs (IR-G02, 21, and 35) competent for accepting bulky amine substrates. IR-G02 shows an excellent substrate scope, which is applied to synthesize over 135 amine molecules as well as a range of APIs' substructures. The crystal structure of IR-G02 reveals the determinants for altering the substrate preference. Finally, we demonstrate a gram-scale synthesis of an analogue of the API sensipar via a kinetic resolution approach, which displays ee >99%, total turnover numbers of up to 2087, and space time yield up to 18.10 g L
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Registered trials
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