ArticleNature communications2015
Non-canonical active site architecture of the radical SAM thiamin pyrimidine synthase.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Insights into the initial steps of the thiamin pyrimidine synthase (ThiC)-catalyzed reaction through EPR spectroscopic characterization of radical intermediates.Chemical science · 2026Article
- Phosphomethylpyrimidine Synthase (ThiC): Trapping of Five Intermediates Provides Mechanistic Insights on a Complex Radical Cascade Reaction in Thiamin Biosynthesis.ACS central science · 2024Article
- Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.Biotechnology for biofuels and bioproducts · 2023Article
- Making and breaking carbon-carbon bonds in class C radical SAM methyltransferases.Journal of inorganic biochemistry · 2022Review
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
- Structural Basis of the Substrate Selectivity of Viperin.Biochemistry · 2020Article
- The plastidialThe Journal of biological chemistry · 2020Article
- Ascorbate and Thiamin: Metabolic Modulators in Plant Acclimation Responses.Plants (Basel, Switzerland) · 2020Review
- An Aminoimidazole Radical Intermediate in the Anaerobic Biosynthesis of the 5,6-Dimethylbenzimidazole Ligand to Vitamin B12.Journal of the American Chemical Society · 2018Article
- C-C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products.Natural product reports · 2018Review
- Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis.Science (New York, N.Y.) · 2018Article
- Structural studies of viperin, an antiviral radical SAM enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Anaerobic 5-Hydroxybenzimidazole Formation from Aminoimidazole Ribotide: An Unanticipated Intersection of Thiamin and Vitamin B₁₂ Biosynthesis.Journal of the American Chemical Society · 2015Article
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6 authors.
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Abstract
Radical S-adenosylmethionine (SAM) enzymes use a [4Fe-4S] cluster to generate a 5'-deoxyadenosyl radical. Canonical radical SAM enzymes are characterized by a β-barrel-like fold and SAM anchors to the differentiated iron of the cluster, which is located near the amino terminus and within the β-barrel, through its amino and carboxylate groups. Here we show that ThiC, the thiamin pyrimidine synthase in plants and bacteria, contains a tethered cluster-binding domain at its carboxy terminus that moves in and out of the active site during catalysis. In contrast to canonical radical SAM enzymes, we predict that SAM anchors to an additional active site metal through its amino and carboxylate groups. Superimposition of the catalytic domains of ThiC and glutamate mutase shows that these two enzymes share similar active site architectures, thus providing strong evidence for an evolutionary link between the radical SAM and adenosylcobalamin-dependent enzyme superfamilies.
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