缺氧诱导因子天冬酰胺羟化酶（FIH-1）催化天冬酰胺803位β-碳原子的羟化反应。
Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
作者信息
McNeill Luke A, Hewitson Kirsty S, Claridge Timothy D, Seibel Jürgen F, Horsfall Louise E, Schofield Christopher J
机构信息
Oxford Centre for Molecular Sciences, Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QY, U.K.
出版信息
Biochem J. 2002 Nov 1;367(Pt 3):571-5. doi: 10.1042/BJ20021162.
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.
摘要
在常氧条件下，人缺氧诱导因子（HIF）-1α亚基C端反式激活结构域中的天冬酰胺803被HIF-1抑制因子（FIH-1）羟基化，导致HIF-1α/p300相互作用被消除。对体外产生的羟基化HIF片段的核磁共振及其他分析表明，羟基化发生在天冬酰胺803的β-碳上，意味着产生苏阿糖型异构体，这与产生赤藓糖型异构体的其他已知天冬氨酸/天冬酰胺羟化酶相反。
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