Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate
LA McNeill, E Flashman, MRG Buck… - Molecular …, 2005 - pubs.rsc.org
LA McNeill, E Flashman, MRG Buck, KS Hewitson, IJ Clifton, G Jeschke, TDW Claridge…
Molecular BioSystems, 2005•pubs.rsc.orgRegulation of the hypoxic response in humans is regulated by the post-translational
hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-
4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity
for, and to copurify with endogenous levels of, its Fe (II) cofactor and 2-oxoglutarate
cosubstrate.
hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-
4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity
for, and to copurify with endogenous levels of, its Fe (II) cofactor and 2-oxoglutarate
cosubstrate.
Regulation of the hypoxic response in humans is regulated by the post-translational hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity for, and to copurify with endogenous levels of, its Fe(II) cofactor and 2-oxoglutarate cosubstrate.
The Royal Society of Chemistry