Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate

被引：99

作者：

McNeill, LA

Flashman, E

Buck, MRG

Hewitson, KS

Clifton, IJ

Jeschke, G

Claridge, TDW

Ehrismann, D

Oldham, NJ

Schofield, CJ

机构：

[1] Univ Oxford, Dept Chem, Oxford OX1 3TA, England

[2] Univ Oxford, Oxford Ctr Mol Sci, Chem Res Lab, Oxford OX1 3TA, England

[3] Max Planck Inst Polymer Res, D-55021 Mainz, Germany

来源：

MOLECULAR BIOSYSTEMS | 2005年 / 1卷 / 04期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

D O I：

10.1039/b511249b

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

收藏

页码：321 / 324

页数：4

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