ArticleChembiochem : a European journal of chemical biology2020
Asymmetric Reduction of (R)-Carvone through a Thermostable and Organic-Solvent-Tolerant Ene-Reductase.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Multigram-Scale Asymmetric Alkene Reduction Catalyzed by a Thermostable Flavin Ene-Reductase.Organic process research & development · 2026Article
- Toward Sustainability: Intensification of Light-Driven Whole Cell Biocatalysis.Chembiochem : a European journal of chemical biology · 2026Review
- Engineering a newly identified alcohol dehydrogenase from Sphingobium Sp. for efficient utilization of nicotinamide cofactors biomimetics.Bioresources and bioprocessing · 2025Article
- Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.Nature communications · 2024Article
- Peroxygenase-Catalyzed Allylic Oxidation Unlocks Telescoped Synthesis of (1ACS catalysis · 2024Article
- Article
- Identification of a novel ene reductase fromRSC advances · 2022Article
- Tunable Production of (ACS catalysis · 2022Article
- Cell-Free Noncanonical Redox Cofactor Systems.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Screening a Strain ofMolecules (Basel, Switzerland) · 2021Article
- Asymmetric Reduction of (R)-Carvone through a Thermostable and Organic-Solvent-Tolerant Ene-Reductase.Chembiochem : a European journal of chemical biology · 2020Article
Corrections and comments
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Authors and funding
7 authors.
Funding
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Abstract
Ene-reductases allow regio- and stereoselective reduction of activated C=C double bonds at the expense of nicotinamide adenine dinucleotide cofactors [NAD(P)H]. Biological NAD(P)H can be replaced by synthetic mimics to facilitate enzyme screening and process optimization. The ene-reductase FOYE-1, originating from an acidophilic iron oxidizer, has been described as a promising candidate and is now being explored for applied biocatalysis. Biological and synthetic nicotinamide cofactors were evaluated to fuel FOYE-1 to produce valuable compounds. A maximum activity of (319.7±3.2) U mg
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