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Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Lancaster, David E. McDonough, Michael A. Schofield, Christopher J. |
| Copyright Year | 2004 |
| Abstract | FIH (Factor inhibiting hypoxia-inducible factor), an asparaginyl beta-hydroxylase belonging to the super-family of 2-oxoglutarate and Fe(II)-dependent dioxygenases, catalyses hydroxylation of Asn-803 of hypoxia-inducible factor, a transcription factor that regulates the mammalian hypoxic response. Only one other asparaginyl beta-hydroxylase, which catalyses hydroxylation of both aspartyl and asparaginyl residues in EGF (epidermal growth factor)-like domains, has been characterized. In the light of recent crystal structures of FIH, we compare FIH with the EGFH (EGF beta-hydroxylase) and putative asparagine/asparaginyl hydroxylases. Sequence analyses imply that EGFH does not contain the HXD/E iron-binding motif characteristic of most of the 2-oxoglutarate oxygenases. |
| File Format | PDF HTM / HTML |
| DOI | 10.1042/BST0320943 |
| PubMed reference number | 15506931 |
| Journal | Medline |
| Volume Number | 32 |
| Part | 6 |
| Alternate Webpage(s) | http://www.biochemsoctrans.org/content/ppbiost/32/6/943.full.pdf |
| Journal | Biochemical Society transactions |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
