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

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

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1
Oxford Centre for Molecular Sciences, Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QY, U.K.

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.

PMID:
12215170
PMCID:
PMC1222951
DOI:
10.1042/BJ20021162
[Indexed for MEDLINE]
Free PMC Article
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