2-Oxoglutarate oxygenases are inhibited by a range of transition metals

Metallomics. 2010 Jun;2(6):397-9. doi: 10.1039/c004952b. Epub 2010 May 20.

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.

MeSH terms

  • Binding, Competitive
  • Coenzymes / pharmacology*
  • Enzyme Activation / drug effects*
  • Histone Demethylases / antagonists & inhibitors
  • Humans
  • Inhibitory Concentration 50
  • Ketoglutaric Acids* / antagonists & inhibitors
  • Oxygenases / antagonists & inhibitors*
  • Procollagen-Proline Dioxygenase / antagonists & inhibitors
  • Transition Elements / pharmacology*

Substances

  • Coenzymes
  • Ketoglutaric Acids
  • Transition Elements
  • Oxygenases
  • Histone Demethylases
  • Procollagen-Proline Dioxygenase