Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate
- 22 August 2005
- journal article
- Published by Royal Society of Chemistry (RSC) in Molecular BioSystems
- Vol. 1 (4), 321-324
- https://doi.org/10.1039/b511249b
Abstract
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.Keywords
This publication has 24 references indexed in Scilit:
- Hydroxylation of HIF-1: Oxygen Sensing at the Molecular LevelPhysiology, 2004
- Oxygen sensing by HIF hydroxylasesNature Reviews Molecular Cell Biology, 2004
- Oxygen sensing in the hypoxic response pathway: regulation of the hypoxia-inducible transcription factorGenes & Development, 2003
- HIF hydroxylation and the mammalian oxygen-sensing pathwayJCI Insight, 2003
- Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803Biochemical Journal, 2002
- The use of dioxygen by HIF prolyl hydroxylase (PHD1)Bioorganic & Medicinal Chemistry Letters, 2002
- A Conserved Family of Prolyl-4-Hydroxylases That Modify HIFScience, 2001
- C. elegans EGL-9 and Mammalian Homologs Define a Family of Dioxygenases that Regulate HIF by Prolyl HydroxylationCell, 2001
- HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 SensingScience, 2001
- Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl HydroxylationScience, 2001