ArticleBiochemistry2016
Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- The Oxidase Reaction of Flavin-Dependent Thymidylate Synthase Reveals the Nature of Inhibitor Binding.Biochemistry · 2025Article
- Selective Inhibitor Design against Thymidylate Synthase ofACS omega · 2025Article
- Structural Plasticity of Flavin-Dependent Thymidylate Synthase Controlled by the Enzyme Redox State.Biomolecules · 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
- An enzymatic activation of formaldehyde for nucleotide methylation.Nature communications · 2021Article
- Mechanism of Naphthoquinone Selectivity of Thymidylate Synthase ThyX.Biophysical journal · 2020Article
- dUMP/F-dUMP Binding to Thymidylate Synthase: Human VersusACS omega · 2020Article
- Experimental and Computational Studies Delineate the Role of Asparagine 177 in Hydride Transfer for E. coli Thymidylate Synthase.ACS catalysis · 2018Article
- Chemo-enzymatic synthesis of the exocyclic olefin isomer of thymidine monophosphate.Bioorganic & medicinal chemistry · 2018Article
- Unique Features and Anti-microbial Targeting of Folate- and Flavin-Dependent Methyltransferases Required for Accurate Maintenance of Genetic Information.Frontiers in microbiology · 2018Review
- Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier.Archives of biochemistry and biophysics · 2017Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Many microorganisms use flavin-dependent thymidylate synthase (FDTS) to synthesize the essential nucleotide 2'-deoxythymidine 5'-monophosphate (dTMP) from 2'-deoxyuridine 5'-monophosphate (dUMP), 5,10-methylenetetrahydrofolate (CH2THF), and NADPH. FDTSs have a structure that is unrelated to the thymidylate synthase used by humans and a very different mechanism. Here we report nuclear magnetic resonance evidence that FDTS ionizes N3 of dUMP using an active-site arginine. The ionized form of dUMP is largely responsible for the changes in the flavin absorbance spectrum of FDTS upon dUMP binding. dUMP analogues also suggest that the phosphate of dUMP acts as the base that removes the proton from C5 of the dUMP-methylene intermediate in the FDTS-catalyzed reaction. These findings establish additional differences between the mechanisms of FDTS and human thymidylate synthase.
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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.