ArticleProceedings of the National Academy of Sciences of the United States of America2013
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 75 citations in OpenAlex.
- Mechanistic insight into radicalNatural product reports · 2026Review
- The Radical SAM Enzyme BlsE Can Operate as a Dehydratase, Dehydrogenase, or Epimerase upon Mutation of a Single Active Site Serine Residue.Journal of the American Chemical Society · 2026Article
- Profile of Catherine Drennan.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanistic Insights from the Crystal Structure and Computational Analysis of the Radical SAM Deaminase DesII.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- Cluster-selectiveChemical science · 2023Article
- Twenty Years of Radical SAM! The Genesis of the Superfamily.ACS bio & med chem Au · 2022Article
- Point mutation of V252 in neomycin C epimerase enlarges substrate-binding pocket and improves neomycin B accumulation in Streptomyces fradiae.Bioresources and bioprocessing · 2022Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Cobalamin-Dependent RadicalACS bio & med chem Au · 2022Review
- Dioxane Bridge Formation during the Biosynthesis of Spectinomycin Involves a Twitch RadicalJournal of the American Chemical Society · 2022Article
- Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes.Current opinion in chemical biology · 2022Review
- Resolving the Multidecade-Long Mystery in MoaA Radical SAM Enzyme Reveals New Opportunities to Tackle Human Health Problems.ACS bio & med chem Au · 2022Review
- How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery.ACS bio & med chem Au · 2022Review
- Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy.Applied magnetic resonance · 2022Review
- HygY Is a Twitch Radical SAM Epimerase with Latent Dehydrogenase Activity Revealed upon Mutation of a Single Cysteine Residue.Journal of the American Chemical Society · 2021Article
- Eukaryotic TYW1 Is a Radical SAM Flavoenzyme.Biochemistry · 2021Article
- Radical SAM Enzymes and Ribosomally-Synthesized and Post-translationally Modified Peptides: A Growing Importance in the Microbiomes.Frontiers in chemistry · 2021Review
- Mechanism of Rate Acceleration of Radical C-C Bond Formation Reaction by a Radical SAM GTP 3',8-Cyclase.Journal of the American Chemical Society · 2020Article
- Analysis of Electrochemical Properties ofJournal of the American Chemical Society · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The 2-deoxy-scyllo-inosamine (DOIA) dehydrogenases are key enzymes in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. In contrast to most DOIA dehydrogenases, which are NAD-dependent, the DOIA dehydrogenase from Bacillus circulans (BtrN) is an S-adenosyl-l-methionine (AdoMet) radical enzyme. To examine how BtrN employs AdoMet radical chemistry, we have determined its structure with AdoMet and substrate to 1.56 Å resolution. We find a previously undescribed modification to the core AdoMet radical fold: instead of the canonical (β/α)6 architecture, BtrN displays a (β5/α4) motif. We further find that an auxiliary [4Fe-4S] cluster in BtrN, thought to bind substrate, is instead implicated in substrate-radical oxidation. High structural homology in the auxiliary cluster binding region between BtrN, fellow AdoMet radical dehydrogenase anSME, and molybdenum cofactor biosynthetic enzyme MoaA provides support for the establishment of an AdoMet radical structural motif that is likely common to ~6,400 uncharacterized AdoMet radical enzymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.