Cited by 215Cancer, Hypoxia, and MetabolismMetal-Catalyzed Oxygenation MechanismsAmino Acid Enzymes and Metabolism

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

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McNEILL, Luke A., HEWITSON, Kirsty S., CLARIDGE, Timothy D., SEIBEL, Jürgen F., HORSFALL, Louise E., SCHOFIELD, Christopher J.·2002·Biochemical Journal

DOI 10.1042/bj20021162PMC PMC1222951

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Abstract

Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 α-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1α/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the β-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.

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Authors: McNEILL, L. A., HEWITSON, K. S., CLARIDGE, T. D., SEIBEL, J. F., HORSFALL, L. E., & SCHOFIELD, C. J.
Affiliations: University of Oxford (GB)
ORCID: CLARIDGE, Timothy D.
SEIBEL, Jürgen F.
HORSFALL, Louise E.
SCHOFIELD, Christopher J.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2002-11-01
Volume: 367
Issue: 3
Pages: 571-575
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20021162
PMC: PMC1222951
OpenAlex: W1999204839
Cited by: 215
References: 29
Citations by year: 2026: 6 · 2025: 5 · 2024: 6 · 2023: 13 · 2022: 12 · 2021: 12 · 2020: 6 · 2019: 5 · 2018: 5 · 2017: 11 · 2016: 7 · 2015: 6 · 2014: 8 · 2013: 7 · 2012: 7
FWCI: 6.37
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
European Commission
Directorate for Biological Sciences
Medical Research Council
Engineering and Physical Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords: FIH-1, asparaginyl hydroxylase, hypoxia-inducible factor-1α, HIF-1α, threo isomer, C-terminal transactivation domain, normoxic conditions
MeSH terms: Amino Acid Sequence, Asparagine, Carbon, Catalysis, DNA-Binding Proteins, Hydroxylation, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Transcription Factors, Nuclear Magnetic Resonance, Biomolecular, Hypoxia-Inducible Factor 1

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

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