Hypoxia-inducible factor-asparagine dioxygenase
| Hypoxia-inducible factor-asparagine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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 hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
Hypoxia-inducible factor-asparagine dioxygenase contains iron, and requires ascorbate.
References
- ↑ Mahon, P.C.; Hirota, K.; Semenza, G.L. (2001). "FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity". Genes Dev. 15 (20): 2675–2686. doi:10.1101/gad.924501. PMC 312814
. PMID 11641274. - ↑ Hewitson, K.S.; McNeill, L.A.; Riordan, M.V.; Tian, Y.M.; Bullock, A.N.; Welford, R.W.; Elkins, J.M.; Oldham, N.J.; Bhattacharya, S.; Gleadle, J.M.; Ratcliffe, P.J.; Pugh, C.W.; Schofield, C.J. (2002). "Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family". J. Biol. Chem. 277 (29): 26351–26355. doi:10.1074/jbc.C200273200. PMID 12042299.
- ↑ Dann, C.E.; Bruick, R.K.; Deisenhofer, J. (2002). "Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway". Proc. Natl. Acad. Sci. USA. 99 (24): 15351–15356. Bibcode:2002PNAS...9915351D. doi:10.1073/pnas.202614999. PMC 137720. PMID 12432100.
- ↑ Lando, D.; Peet, D.J.; Whelan, D.A.; Gorman, J.J.; Whitelaw, M.L. (2002). "Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch". Science. 295 (5556): 858–861. Bibcode:2002Sci...295..858L. doi:10.1126/science.1068592. PMID 11823643.
- ↑ Koivunen, P.; Hirsila, M.; Gunzler, V.; Kivirikko, K.I.; Myllyharju, J. (2004). "Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases". J. Biol. Chem. 279 (11): 9899–9904. doi:10.1074/jbc.M312254200. PMID 14701857.
- ↑ Elkins, J.M.; Hewitson, K.S.; McNeill, L.A.; Seibel, J.F.; Schlemminger, I.; Pugh, C.W.; Ratcliffe, P.J.; Schofield, C.J. (2003). "Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 α". J. Biol. Chem. 278 (3): 1802–1806. 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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