Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

Biochem J. 2002 Nov 1;367(Pt 3):571-5. doi: 10.1042/BJ20021162.


Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo -isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro -isomer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Asparagine / metabolism*
  • Carbon / metabolism*
  • Catalysis
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Hydroxylation
  • Hypoxia-Inducible Factor 1
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Transcription Factors*


  • DNA-Binding Proteins
  • Hypoxia-Inducible Factor 1
  • Nuclear Proteins
  • Transcription Factors
  • Asparagine
  • Carbon