ArticleNature communications2021
An enzymatic activation of formaldehyde for nucleotide methylation.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Petromaroside A, an unprecedented natural nucleoside from the spongeRSC advances · 2026Article
- A Riboflavin-Derived Flavinium Salt Mediates Chemoselective Methylation Reactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Prebiotic Roles of Formaldehyde as an Activating Agent and a Building Block in Solid-State Peptide Modification.ACS bio & med chem Au · 2025Article
- Formaldehyde and its surrogates as a C1 platform for defossilised modern societies.Chemical Society reviews · 2025Review
- Bioinspired transfer methylation enabled by a photoactive reagent.Nature communications · 2025Article
- Proteomic analysis of Antarctic sea-ice yeast Rhodotorula mucilaginosa AN5 responding to hyper- and hyposalinity stress.World journal of microbiology & biotechnology · 2025Article
- Structural Plasticity of Flavin-Dependent Thymidylate Synthase Controlled by the Enzyme Redox State.Biomolecules · 2025Article
- Diatom volatile organic compound production is driven by diel metabolism and the cell cycle.Frontiers in microbiology · 2025Article
- Insights into the Mechanism of Installation of 5-Carboxymethylaminomethyl Uridine Hypermodification by tRNA-Modifying Enzymes MnmE and MnmG.Journal of the American Chemical Society · 2023Article
- Integrative Approach to Probe Alternative Redox Mechanisms in RNA Modifications.Accounts of chemical research · 2023Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Folate enzyme cofactors and their derivatives have the unique ability to provide a single carbon unit at different oxidation levels for the de novo synthesis of amino-acids, purines, or thymidylate, an essential DNA nucleotide. How these cofactors mediate methylene transfer is not fully settled yet, particularly with regard to how the methylene is transferred to the methylene acceptor. Here, we uncovered that the bacterial thymidylate synthase ThyX, which relies on both folate and flavin for activity, can also use a formaldehyde-shunt to directly synthesize thymidylate. Combining biochemical, spectroscopic and anaerobic crystallographic analyses, we showed that formaldehyde reacts with the reduced flavin coenzyme to form a carbinolamine intermediate used by ThyX for dUMP methylation. The crystallographic structure of this intermediate reveals how ThyX activates formaldehyde and uses it, with the assistance of active site residues, to methylate dUMP. Our results reveal that carbinolamine species promote methylene transfer and suggest that the use of a CH
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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.