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

L A McNeill, K S Hewitson, T D Claridge, J F Seibel, L E Horsfall, C J Schofield

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)571-575
Number of pages5
JournalBiochemical Journal
Volume367
DOIs
Publication statusPublished - 1 Nov 2002

Keywords

  • asparagine hydroxylation
  • factor inhibiting hypoxia-inducible factor-1 (FIH-1)
  • hypoxia
  • oxygenase
  • oxygen sensing

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