{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Simelis K"],"funding":["RCUK | Engineering and Physical Sciences Research Council (EPSRC)","Cancer Research UK","EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)"],"pagination":["305"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11662004"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["Fe(II)- and 2-oxoglutarate (2OG)-dependent dioxygenases use 2OG and O<sub>2</sub> cofactors to catalyse substrate oxidation and yield oxidised product, succinate, and CO<sub>2</sub>. Simultaneous detection of substrate and cofactors is difficult, contributing to a poor understanding of the dynamics between substrate oxidation and 2OG decarboxylation activities. Here, we profile 5-methylcytosine (<sup>5m</sup>C)-oxidising Ten-Eleven Translocation (TET) enzymes using MS and <sup>1</sup>H NMR spectroscopy methods and reveal a high degree of substrate oxidation-independent 2OG turnover under a range of conditions. 2OG decarboxylase activity is substantial (>20% 2OG turned over after 1 h) in the absence of substrate, while, under substrate-saturating conditions, half of total 2OG consumption is"],"journal":["Communications chemistry"],"pubmed_title":["Unravelling 2-oxoglutarate turnover and substrate oxidation dynamics in 5-methylcytosine-oxidising TET enzymes."],"pmcid":["PMC11662004"],"funding_grant_id":["101003111","C8717/A28285","EP/L015838/1"],"pubmed_authors":["Kawamura A","Simelis K","Belle R"],"additional_accession":[]},"is_claimable":false,"name":"Unravelling 2-oxoglutarate turnover and substrate oxidation dynamics in 5-methylcytosine-oxidising TET enzymes.","description":"Fe(II)- and 2-oxoglutarate (2OG)-dependent dioxygenases use 2OG and O<sub>2</sub> cofactors to catalyse substrate oxidation and yield oxidised product, succinate, and CO<sub>2</sub>. Simultaneous detection of substrate and cofactors is difficult, contributing to a poor understanding of the dynamics between substrate oxidation and 2OG decarboxylation activities. Here, we profile 5-methylcytosine (<sup>5m</sup>C)-oxidising Ten-Eleven Translocation (TET) enzymes using MS and <sup>1</sup>H NMR spectroscopy methods and reveal a high degree of substrate oxidation-independent 2OG turnover under a range of conditions. 2OG decarboxylase activity is substantial (>20% 2OG turned over after 1 h) in the absence of substrate, while, under substrate-saturating conditions, half of total 2OG consumption is","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2025-04-25T21:27:12.31Z","creation":"2025-04-06T08:48:38.193Z"},"accession":"S-EPMC11662004","cross_references":{"pubmed":["39706884"],"doi":["10.1038/s42004-024-01382-1"]}}