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Hypoxia-inducible factor-asparagine dioxygenase

From Wikipedia, the free encyclopedia

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

  1. ^ Mahon PC, Hirota K, Semenza GL (October 2001). "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. doi:10.1101/gad.924501. PMC 312814. PMID 11641274.
  2. ^ Hewitson KS, McNeill LA, Riordan MV, Tian YM, Bullock AN, Welford RW, Elkins JM, Oldham NJ, Bhattacharya S, Gleadle JM, Ratcliffe PJ, Pugh CW, Schofield CJ (July 2002). "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. doi:10.1074/jbc.C200273200. PMID 12042299.
  3. ^ Dann CE, Bruick RK, Deisenhofer J (November 2002). "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. Bibcode:2002PNAS...9915351D. doi:10.1073/pnas.202614999. PMC 137720. PMID 12432100.
  4. ^ Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML (February 2002). "Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch". Science. 295 (5556): 858–61. Bibcode:2002Sci...295..858L. doi:10.1126/science.1068592. PMID 11823643. S2CID 24045310.
  5. ^ Koivunen P, Hirsilä M, Günzler V, Kivirikko KI, Myllyharju J (March 2004). "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. doi:10.1074/jbc.M312254200. PMID 14701857.
  6. ^ Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ (January 2003). "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. doi:10.1074/jbc.C200644200. PMID 12446723.

External links

This page was last edited on 26 August 2023, at 14:31
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