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Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
| Content Provider | Semantic Scholar |
|---|---|
| Author | McNeill, Luke A. Hewitson, Kirsty S. Claridge, Timothy D. W. Seibel, Jürgen F. Horsfall, Louise E. Schofield, Christopher J. |
| Copyright Year | 2002 |
| Abstract | Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo -isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro -isomer. |
| File Format | PDF HTM / HTML |
| DOI | 10.1042/BJ20021162 |
| PubMed reference number | 12215170 |
| Journal | Medline |
| Volume Number | 367 |
| Part | 3 |
| Alternate Webpage(s) | http://www.biochemj.org/content/ppbiochemj/367/3/571.full.pdf |
| Alternate Webpage(s) | https://doi.org/10.1042/BJ20021162 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |