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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO₂

Hypoxia-inducible factor-asparagine dioxygenase contains iron, and requires ascorbate.

References

1. Mahon, P.C., Hirota, K. and 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.
2. 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. and 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.
3. Dann, C.E., 3rd, Bruick, R.K. and Deisenhofer, J.; Bruick; Deisenhofer (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.
4. Lando, D., Peet, D.J., Whelan, D.A., Gorman, J.J. and Whitelaw, M.L.; Peet; Whelan; Gorman; Whitelaw (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.
5. Koivunen, P., Hirsila, M., Gunzler, V., Kivirikko, K.I. and 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.
6. Elkins, J.M., Hewitson, K.S., McNeill, L.A., Seibel, J.F., Schlemminger, I., Pugh, C.W., Ratcliffe, P.J. and 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)