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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

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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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