ArticleACS catalysis2020
C=C-Ene-Reductases Reduce the C=N Bond of Oximes.
Article in ACS catalysis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Sustainable Biocatalytic Cascades: A Versatile Tool in the Synthesis of Natural Products With Therapeutic Potential.Chembiochem : a European journal of chemical biology · 2026Review
- Structure, Oligomerization, and Thermal Stability of a Recently Discovered Old Yellow Enzyme.Proteins · 2025Article
- Asymmetric Monoreduction of α,β-Dicarbonyls to α-Hydroxy Carbonyls by Ene Reductases.ACS catalysis · 2024Article
- Enantioselective Transfer Hydrogenation of α-Methoxyimino-β-keto Esters.The Journal of organic chemistry · 2024Article
- Unlocking the function promiscuity of old yellow enzyme to catalyze asymmetric Morita-Baylis-Hillman reaction.Nature communications · 2024Article
- Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.Nature communications · 2024Article
- Multifunctional Biocatalysts for Organic Synthesis.Journal of the American Chemical Society · 2024Review
- Deciphering the Unconventional Reduction of C=N Bonds by Old Yellow Enzymes Using QM/MM.ACS catalysis · 2024Article
- Mechanistic Insights into the Ene-Reductase-Catalyzed Promiscuous Reduction of Oximes to Amines.ACS catalysis · 2023Article
- Article
- Catalytic Reduction of Oximes to Hydroxylamines: Current Methods, Challenges and Opportunities.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Review
- Direct Conversion of Hydrazones to Amines using Transaminases.ChemCatChem · 2021Article
- Imine reduction by an Ornithine cyclodeaminase/μ-crystallin homolog purified fromBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Enzymatic strategies for asymmetric synthesis.RSC chemical biology · 2021Review
- Predicting enzymatic reactions with a molecular transformer.Chemical science · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although enzymes have been found for many reactions, there are still transformations for which no enzyme is known. For instance, not a single defined enzyme has been described for the reduction of the C=N bond of an oxime, only whole organisms. Such an enzymatic reduction of an oxime may give access to (chiral) amines. By serendipity, we found that the oxime moiety adjacent to a ketone as well as an ester group can be reduced by ene-reductases (ERs) to an intermediate amino group. ERs are well-known enzymes for the reduction of activated alkenes, as of α,β-unsaturated ketones. For the specific substrate used here, the amine intermediate spontaneously reacts further to tetrasubstituted pyrazines. This reduction reaction represents an unexpected promiscuous activity of ERs expanding the toolkit of transformations using enzymes.
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Registered trials
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