The use of dioxygen by HIF prolyl hydroxylase (PHD1)

Bioorg Med Chem Lett. 2002 Jun 17;12(12):1547-50. doi: 10.1016/s0960-894x(02)00219-6.

Abstract

The hypoxic response in animals is mediated by hydroxylation of proline residues in the alpha-subunit of hypoxia inducible factor (HIF). Hydroxylation is catalysed by prolyl-4-hydroxylases (PHD isozymes in humans) which are iron(II) and 2-oxoglutarate dependent oxygenases. Mutation of the arginine proposed to bind 2-oxoglutarate and of the 2His-1-carboxylate iron(II) binding motif in PHD1 dramatically reduces its activity. The source of the oxygen of the product alcohol is (>95%) dioxygen.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Humans
  • Hydroxylation
  • Molecular Sequence Data
  • Oxygen / metabolism*
  • Procollagen-Proline Dioxygenase / chemistry
  • Procollagen-Proline Dioxygenase / metabolism*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Procollagen-Proline Dioxygenase
  • Oxygen