ArticleBiochemistry2013
Spectroscopic, steady-state kinetic, and mechanistic characterization of the radical SAM enzyme QueE, which catalyzes a complex cyclization reaction in the biosynthesis of 7-deazapurines.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 68 citations in OpenAlex.
- Mechanistic insight into radicalNatural product reports · 2026Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Initiation, Propagation, and Termination in the Chemistry of Radical SAM Enzymes.Biochemistry · 2024Review
- Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator.PLoS genetics · 2024Article
- Macrocyclization and Backbone Rearrangement During RiPP Biosynthesis by a SAM-Dependent Domain-of-Unknown-Function 692.ACS central science · 2023Article
- Metal retention and replacement in QueD2 protect queuosine-tRNA biosynthesis in metal-starvedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- Journey on the Radical SAM Road as an Accidental Pilgrim.ACS bio & med chem Au · 2022Review
- Article
- New Role for Radical SAM Enzymes in the Biosynthesis of Thio(seleno)oxazole RiPP Natural Products.Biochemistry · 2021Article
- tRNA Modifications as a Readout of S and Fe-S Metabolism.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Analysis of Electrochemical Properties ofJournal of the American Chemical Society · 2019Article
- Metabolic functions of the human gut microbiota: the role of metalloenzymes.Natural product reports · 2019Review
- Crystal structure of AdoMet radical enzyme 7-carboxy-7-deazaguanine synthase from Escherichia coli suggests how modifications near [4Fe-4S] cluster engender flavodoxin specificity.Protein science : a publication of the Protein Society · 2019Article
- Calditol-linked membrane lipids are required for acid tolerance inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Radical Clock Probe Uncouples H Atom Abstraction from Thioether Cross-Link Formation by the Radical S-Adenosyl-l-methionine Enzyme SkfB.Biochemistry · 2018Article
- Following the electrons: peculiarities in the catalytic cycles of radical SAM enzymes.Natural product reports · 2018Review
- X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.Biochemistry · 2018Article
- A Radical Intermediate in Bacillus subtilis QueE during Turnover with the Substrate Analogue 6-Carboxypterin.Journal of the American Chemical Society · 2018Article
- QueE: A Radical SAM Enzyme Involved in the Biosynthesis of 7-Deazapurine Containing Natural Products.Methods in enzymology · 2018Article
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3 authors at 2 institutions in 1 country.
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Abstract
7-Carboxy-7-deazaguanine (CDG) synthase (QueE) catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH(4)) to CDG in the third step of the biosynthetic pathway to all 7-deazapurines. Here we present a detailed characterization of QueE from Bacillus subtilis to delineate the mechanism of conversion of CPH(4) to CDG. QueE is a member of the radical S-adenosyl-l-methionine (SAM) superfamily, all of which use a bound [4Fe-4S](+) cluster to catalyze the reductive cleavage of the SAM cofactor to generate methionine and a 5'-deoxyadenosyl radical (5'-dAdo(•)), which initiates enzymatic transformations requiring hydrogen atom abstraction. The ultraviolet-visible, electron paramagnetic resonance, and Mössbauer spectroscopic features of the homodimeric QueE point to the presence of a single [4Fe-4S] cluster per monomer. Steady-state kinetic experiments indicate a K(m) of 20 ± 7 μM for CPH(4) and a k(cat) of 5.4 ± 1.2 min(-1) for the overall transformation. The kinetically determined K(app) for SAM is 45 ± 1 μM. QueE is also magnesium-dependent and exhibits a K(app) for the divalent metal ion of 0.21 ± 0.03 mM. The SAM cofactor supports multiple turnovers, indicating that it is regenerated at the end of each catalytic cycle. The mechanism of rearrangement of QueE was probed with CPH(4) isotopologs containing deuterium at C-6 or the two prochiral positions at C-7. These studies implicate 5'-dAdo(•) as the initiator of the ring contraction reaction catalyzed by QueE by abstraction of the H atom from C-6 of CPH(4).
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