ArticleAnalytical biochemistry2017
A rapid mass spectrometric method for the measurement of catalytic activity of ten-eleven translocation enzymes.
Article in Analytical biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- DREAMS illuminates spatial DNA and RNA modification landscapes.Nature cell biology · 2026Article
- Nitric oxide inhibits ten-eleven translocation DNA demethylases to regulate 5mC and 5hmC across the genome.Nature communications · 2025Article
- Analogue-Sensitive Inhibition of Histone Demethylases Uncovers Member-Specific Function in Ribosomal Protein Synthesis.Journal of the American Chemical Society · 2025Article
- Unravelling 2-oxoglutarate turnover and substrate oxidation dynamics in 5-methylcytosine-oxidising TET enzymes.Communications chemistry · 2024Article
- Robust Bisulfite-Free Single-Molecule Real-Time Sequencing of Methyldeoxycytidine Based on a Novel hpTet3 Enzyme.Angewandte Chemie (International ed. in English) · 2024Article
- Nitric oxide inhibits ten-eleven translocation DNA demethylases to regulate 5mC and 5hmC across the genome.Research square · 2024Article
- Focused Screening Identifies Different Sensitivities of Human TET Oxygenases to the Oncometabolite 2-Hydroxyglutarate.Journal of medicinal chemistry · 2024Article
- Development of a rapid mass spectrometric method for the analysis of ten-eleven translocation enzymes.Methods in enzymology · 2024Article
- Oxime formation coordination-directed detection of genome-wide thymine oxides with nanogram-scale sample input.Chemical science · 2022Article
- Catalytic Space Engineering as a Strategy to Activate C-H Oxidation on 5-Methylcytosine in Mammalian Genome.Journal of the American Chemical Society · 2021Article
- Site- and degree-specific C-H oxidation on 5-methylcytosine homologues for probing active DNA demethylation.Chemical science · 2019Article
- Complementary Steric Engineering at the Protein-Ligand Interface for Analogue-Sensitive TET Oxygenases.Journal of the American Chemical Society · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Enzymatic methylation at carbon five on cytosine (5mC) in DNA is a hallmark of mammalian epigenetic programming and is critical to gene regulation during early embryonic development. It has recently been shown that dynamic erasure of 5mC by three members of the ten-eleven translocation (TET) family plays a key role in cellular differentiation. TET enzymes belong to Fe (II)- and 2-ketoglutarate (2KG) dependent dioxygenases that successively oxidize 5mC to 5-hydroxymethyl cytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxycytosine (5CaC), thus providing a chemical basis for the removal of 5mC which once was thought to be a permanent mark in mammalian genome. Since then a wide range of biochemical assays have been developed to characterize TET activity. Majority of these methods require multi-step processing to detect and quantify the TET-mediated oxidized products. In this study, we have developed a MALDI mass spectrometry based method that directly measures the TET activity with high sensitivity while eliminating the need for any intermediate processing steps. We applied this method to the measurement of enzymatic activity of TET2 and 3, Michaleis-Menten parameters (K
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