[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/hypoxia-inducible-factor-asparagine-dioxygenase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/hypoxia-inducible-factor-asparagine-dioxygenase-wikipedia\/","headline":"Hypoxia-inducible factor-asparagine dioxygenase – Wikipedia","name":"Hypoxia-inducible factor-asparagine dioxygenase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Hypoxia-inducible factor-asparagine dioxygenase (EC 1.14.11.30, HIF hydroxylase) is an enzyme with systematic name","datePublished":"2022-09-16","dateModified":"2022-09-16","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/hypoxia-inducible-factor-asparagine-dioxygenase-wikipedia\/","about":["Wiki"],"wordCount":3157,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Hypoxia-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\u21cc{displaystyle rightleftharpoons } hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2Hypoxia-inducible factor-asparagine dioxygenase contains iron, and requires ascorbate.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4References[edit]^ 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\u201386. doi:10.1101\/gad.924501. PMC\u00a0312814. PMID\u00a011641274.^ 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\u20135. doi:10.1074\/jbc.C200273200. PMID\u00a012042299.^ 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\u20136. Bibcode:2002PNAS…9915351D. doi:10.1073\/pnas.202614999. PMC\u00a0137720. PMID\u00a012432100.^ 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\u201361. Bibcode:2002Sci…295..858L. doi:10.1126\/science.1068592. PMID\u00a011823643. S2CID\u00a024045310.^ Koivunen P, Hirsil\u00e4 M, G\u00fcnzler 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\u2013904. doi:10.1074\/jbc.M312254200. PMID\u00a014701857.^ 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\u20136. doi:10.1074\/jbc.C200644200. 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