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. 2002 Nov 1;367(Pt 3):571-5.
doi: 10.1042/BJ20021162.

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

Luke A McNeill  1 , Kirsty S Hewitson, Timothy D Claridge, Jürgen F Seibel, Louise E Horsfall, Christopher J Schofield
Affiliations

"V体育安卓版" Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

Luke A McNeill et al. Biochem J. .

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 VSports手机版. .

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