ArticleProtein science : a publication of the Protein Society2019
Crystal structure of AdoMet radical enzyme 7-carboxy-7-deazaguanine synthase from Escherichia coli suggests how modifications near [4Fe-4S] cluster engender flavodoxin specificity.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator.PLoS genetics · 2024Article
- Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024Review
- Evidence for Porphyrin-Mediated Electron Transfer in the Radical SAM Enzyme HutW.Biochemistry · 2023Article
- The absence of the queuosine tRNA modification leads to pleiotropic phenotypes revealing perturbations of metal and oxidative stress homeostasis in Escherichia coli K12.Metallomics : integrated biometal science · 2022Article
- Journey on the Radical SAM Road as an Accidental Pilgrim.ACS bio & med chem Au · 2022Review
- Eukaryotic TYW1 Is a Radical SAM Flavoenzyme.Biochemistry · 2021Article
- Analysis of Electrochemical Properties ofJournal of the American Chemical Society · 2019Article
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Authors and funding
7 authors.
Funding
Abstract
7-Carboxy-7-deazaguanine synthase, QueE, catalyzes the radical mediated ring contraction of 6-carboxy-5,6,7,8-tetrahydropterin, forming the characteristic pyrrolopyrimidine core of all 7-deazaguanine natural products. QueE is a member of the S-adenosyl-L-methionine (AdoMet) radical enzyme superfamily, which harnesses the reactivity of radical intermediates to perform challenging chemical reactions. Members of the AdoMet radical enzyme superfamily utilize a canonical binding motif, a CX
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