ArticleAngewandte Chemie (International ed. in English)2015
Mechanistic studies of the radical S-adenosylmethionine enzyme DesII with TDP-D-fucose.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- Radical Propagation via σ-Cleavage Mediates Radical SAM Catalyzed Sulfur-for-Oxygen Swapping Reaction during the Biosynthesis of Albomycin δJournal of the American Chemical Society · 2025Article
- EPR Characterization of the BlsE Substrate Radical Offers Insight into the Determinants of Reaction Outcome that Distinguish Radical SAM Dioldehydratases from Dehydrogenases.Journal of the American Chemical Society · 2025Article
- Initiation, Propagation, and Termination in the Chemistry of Radical SAM Enzymes.Biochemistry · 2024Review
- Mechanistic Insights from the Crystal Structure and Computational Analysis of the Radical SAM Deaminase DesII.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Mechanistic Investigation of 1,2-Diol Dehydration of Paromamine Catalyzed by the RadicalJournal of the American Chemical Society · 2021Article
- Biosynthetic access to the rare antiarose sugarChemical science · 2020Article
- Mechanistic Implications of the Deamination of TDP-4-amino-4-deoxy-d-fucose Catalyzed by the Radical SAM Enzyme DesII.Biochemistry · 2018Article
- Theory and Application of the Relationship Between Steady-State Isotope Effects on Enzyme Intermediate Concentrations and Net Rate Constants.Methods in enzymology · 2017Article
- Organometallic Complex Formed by an Unconventional Radical S-Adenosylmethionine Enzyme.Journal of the American Chemical Society · 2016Article
- C3'-Deoxygenation of Paromamine Catalyzed by a Radical S-Adenosylmethionine Enzyme: Characterization of the Enzyme AprD4 and Its Reductase Partner AprD3.Angewandte Chemie (International ed. in English) · 2016Article
- Catalytic Promiscuity of the Radical S-adenosyl-L-methionine Enzyme NosL.Frontiers in chemistry · 2016Review
- Mechanistic Investigation of the Radical S-Adenosyl-L-methionine Enzyme DesII Using Fluorinated Analogues.Journal of the American Chemical Society · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
DesII is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the C4-deamination of TDP-4-amino-4,6-dideoxyglucose through a C3 radical intermediate. However, if the C4 amino group is replaced with a hydroxy group (to give TDP-quinovose), the hydroxy group at C3 is oxidized to a ketone with no C4-dehydration. It is hypothesized that hyperconjugation between the C4 C-N/O bond and the partially filled p orbital at C3 of the radical intermediate modulates the degree to which elimination competes with dehydrogenation. To investigate this hypothesis, the reaction of DesII with the C4-epimer of TDP-quinovose (TDP-fucose) was examined. The reaction primarily results in the formation of TDP-6-deoxygulose and likely regeneration of TDP-fucose. The remainder of the substrate radical partitions roughly equally between C3-dehydrogenation and C4-dehydration. Thus, changing the stereochemistry at C4 permits a more balanced competition between elimination and dehydrogenation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.