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Investigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygen.

Abstract:

The prolyl hydroxylase domain proteins (PHDs) catalyse the post-translational hydroxylation of the hypoxia-inducible factor (HIF), a modification that regulates the hypoxic response in humans. The PHDs are Fe(II)/2-oxoglutarate (2OG) oxygenases; their catalysis is proposed to provide a link between cellular HIF levels and changes in O2 availability. Transient kinetic studies have shown that purified PHD2 reacts slowly with O2 compared with some other studied 2OG oxygenases, a property which m...

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Publication status:
Published

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Publisher copy:
10.1042/bj20140779

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Publisher:
Portland Press Ltd
Journal:
The Biochemical journal
Volume:
463
Issue:
3
Pages:
363-372
Publication date:
2014-11-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:473fd2b1-673a-4cbb-927d-7cfb8d83c293
Source identifiers:
481508
Local pid:
pubs:481508

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