缺氧诱导因子脯氨酰羟化酶2对亚铁离子和2-氧代戊二酸具有高亲和力。
Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate.
作者信息
McNeill Luke A, Flashman Emily, Buck Matthew R G, Hewitson Kirsty S, Clifton Ian J, Jeschke Gunnar, Claridge Timothy D W, Ehrismann Dominic, Oldham Neil J, Schofield Christopher J
机构信息
The Department of Chemistry and The Oxford Centre for Molecular Sciences, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, UK.
出版信息
Mol Biosyst. 2005 Oct;1(4):321-4. doi: 10.1039/b511249b. Epub 2005 Aug 22.
Regulation of the hypoxic response in humans is regulated by the post-translational hydroxylation of hypoxia inducible transcription factor; a recombinant form of a human prolyl-4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity for, and to copurify with endogenous levels of, its Fe(ii) cofactor and 2-oxoglutarate cosubstrate.
人类低氧反应的调节是由低氧诱导转录因子的翻译后羟基化作用所调控；一种重组形式的人脯氨酰-4-羟化酶（PHD2）得到了表征，结果显示其对亚铁离子（Fe(ii)）辅因子和2-氧戊二酸共底物具有出人意料的高亲和力，并能与内源性水平的它们一起共纯化。
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