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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.14.11.30

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 1.14.11.30

Enzymes and Genes:
hypoxia-inducible factor-asparagine dioxygenase Inferred from experiment : HIF1AN ( Homo sapiens )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: hypoxia-inducible factor-asparagine dioxygenase

Enzyme Commission Synonyms: HIF hydroxylase

Enzyme Commission Summary:
Contains iron, and requires ascorbate. Catalyses hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-α, the α subunit of the transcriptional regulator HIF (hypoxia-inducible factor), which reduces its interaction with the transcriptional coactivator protein p300. The requirement of oxygen for the hydroxylation reaction enables animals to respond to hypoxia.

Citations: [Dann02, Lando02, Koivunen04, Mahon01, Hewitson02, Elkins03b]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.14.11.30 , ENZYME:EC:1.14.11.30 , IUBMB-ExplorEnz:EC:1.14.11.30

Credits:
Created 15-Mar-2010 by Caspi R , SRI International


References

Dann02: Dann CE, Bruick RK, Deisenhofer J (2002). "Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway." Proc Natl Acad Sci U S A 99(24);15351-6. PMID: 12432100

Elkins03b: Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ (2003). "Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha." J Biol Chem 278(3);1802-6. PMID: 12446723

Hewitson02: 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 (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);26351-5. PMID: 12042299

Koivunen04: Koivunen P, Hirsila M, Gunzler V, Kivirikko KI, 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);9899-904. PMID: 14701857

Lando02: Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML (2002). "Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch." Science 295(5556);858-61. PMID: 11823643

Mahon01: Mahon PC, Hirota K, Semenza GL (2001). "FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity." Genes Dev 15(20);2675-86. PMID: 11641274


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, BIOCYC13B.