Biology:Hypoxia-inducible factor-asparagine dioxygenase
From HandWiki
| Hypoxia-inducible factor-asparagine dioxygenase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.14.11.30 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Hypoxia-inducible factor-asparagine dioxygenase (EC 1.14.11.30, HIF hydroxylase) is an enzyme with systematic name hypoxia-inducible factor-L-asparagine, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction:
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 [math]\displaystyle{ \rightleftharpoons }[/math] hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
Hypoxia-inducible factor-asparagine dioxygenase contains iron, and requires ascorbate.
References
- ↑ "FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity". Genes & Development 15 (20): 2675–86. October 2001. doi:10.1101/gad.924501. PMID 11641274.
- ↑ "Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family". The Journal of Biological Chemistry 277 (29): 26351–5. July 2002. doi:10.1074/jbc.C200273200. PMID 12042299.
- ↑ "Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway". Proceedings of the National Academy of Sciences of the United States of America 99 (24): 15351–6. November 2002. doi:10.1073/pnas.202614999. PMID 12432100. Bibcode: 2002PNAS...9915351D.
- ↑ "Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch". Science 295 (5556): 858–61. February 2002. doi:10.1126/science.1068592. PMID 11823643. Bibcode: 2002Sci...295..858L.
- ↑ "Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases". The Journal of Biological Chemistry 279 (11): 9899–904. March 2004. doi:10.1074/jbc.M312254200. PMID 14701857.
- ↑ "Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha". The Journal of Biological Chemistry 278 (3): 1802–6. January 2003. doi:10.1074/jbc.C200644200. PMID 12446723.
External links
- Hypoxia-inducible+factor-asparagine+dioxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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