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

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.
Publication status:
Published

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Publisher copy:
10.1042/bj20021162

Authors


McNeill, LA More by this author
Hewitson, KS More by this author
Claridge, TD More by this author
Seibel, JF More by this author
Horsfall, LE More by this author
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Journal:
The Biochemical journal
Volume:
367
Issue:
Pt 3
Pages:
571-575
Publication date:
2002-11-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:adbef5f2-e95e-4b67-bfcb-fe9077a00bd3
Source identifiers:
32192
Local pid:
pubs:32192

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