- 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...
Expand abstract - Publication status:
- Published
- 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
- Copyright date:
- 2014
Journal article
Investigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygen.
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