title: 2-Oxoglutarate oxygenases are inhibited by a range of transition metals.
abstract: 2-Oxoglutarate oxygenases are inhibited by a range of transition metals, as exemplified by studies on human histone demethylases and prolyl hydroxylase domain 2 (PHD2 or EGLN1). The biological effects associated with 2-oxoglutarate oxygenase inhibition may result from inhibition of more than one enzyme and by mechanisms in addition to simple competition with the Fe(ii) cofactor.
authors.affiliation: Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UK.
authors.forename: Rok
authors.initials: R
authors.lastname: Sekirnik
authors.forename: Nathan R
authors.initials: NR
authors.lastname: Rose
authors.forename: Jasmin
authors.initials: J
authors.lastname: Mecinović
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D001667:Binding, Competitive; D003067:Coenzymes / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects*; D056466:Histone Demethylases / Q000037:antagonists & inhibitors; D006801:Humans; D020128:Inhibitory Concentration 50; D007656:Ketoglutaric Acids / Q000037:antagonists & inhibitors; D010105:Oxygenases / Q000037:antagonists & inhibitors*; D011393:Procollagen-Proline Dioxygenase / Q000037:antagonists & inhibitors; D028561:Transition Elements / Q000494:pharmacology*
chemical_list: D003067:Coenzymes; D007656:Ketoglutaric Acids; D028561:Transition Elements; D010105:Oxygenases; D056466:Histone Demethylases; D011393:Procollagen-Proline Dioxygenase