ec:1.14.11.n4 : No such data.

EC               Enzyme                                 

hypoxia-inducible factor-asparagine dioxygenase;
HIF hydroxylase
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy
hypoxia-inducible factor-L-asparagine, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 = hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
hypoxia-inducible factor-L-asparagine;
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine;
succinate [CPD:C00042];
CO2 [CPD:C00011]
Contains iron, and requires ascorbate. Catalyses hydroxylation of an asparagine in the C-terminal transcriptional activation domain of HIF-alpha, the alpha 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.
EC created 2010
K18055  hypoxia-inducible factor 1-alpha inhibitor (HIF hydroxylase)
HSA: 55662(HIF1AN)
PTR: 466183(HIF1AN)
PPS: 100969925(HIF1AN)
GGO: 101140559(HIF1AN)
PON: 100450996(HIF1AN)
NLE: 100604492(HIF1AN)
MCC: 710425(HIF1AN)
MCF: 102123484(HIF1AN)
CSAB: 103216391(HIF1AN)
RRO: 104656480(HIF1AN)
RBB: 108535279(HIF1AN)
CJC: 100415279(HIF1AN)
SBQ: 101041386(HIF1AN)
MMU: 319594(Hif1an)
RNO: 309434(Hif1an)
CGE: 100752342(Hif1an)
NGI: 103743986(Hif1an)
HGL: 101715790(Hif1an)
CCAN: 109685931(Hif1an)
OCU: 100347080(HIF1AN)
TUP: 102471470(HIF1AN)
CFA: 609221(HIF1AN)
AML: 100484876(HIF1AN)
UMR: 103677605(HIF1AN)
ORO: 101367069(HIF1AN)
FCA: 101091901(HIF1AN)
PTG: 102952057(HIF1AN)
AJU: 106966868(HIF1AN)
BTA: 520864(HIF1AN)
BOM: 102285023(HIF1AN)
BIU: 109579158(HIF1AN)
PHD: 102341833(HIF1AN)
CHX: 102182662(HIF1AN)
OAS: 101122066(HIF1AN)
SSC: 100155854(HIF1AN)
CFR: 102504253(HIF1AN)
CDK: 105084325(HIF1AN)
BACU: 103010817(HIF1AN)
LVE: 103087616(HIF1AN)
OOR: 101282716(HIF1AN) 101283131
ECB: 100070337(HIF1AN)
EPZ: 103562515(HIF1AN)
EAI: 106846748(HIF1AN)
MYB: 102258997(HIF1AN)
MYD: 102758329(HIF1AN)
HAI: 109379673(HIF1AN)
RSS: 109443948(HIF1AN)
PALE: 102898816(HIF1AN)
LAV: 100665502(HIF1AN)
TMU: 101343053
MDO: 100010508(HIF1AN)
SHR: 100932046(HIF1AN)
OAA: 100084505(HIF1AN)
GGA: 428952(HIF1AN)
MGP: 100547017(HIF1AN)
CJO: 107315863(HIF1AN)
APLA: 101796702(HIF1AN)
ACYG: 106029735(HIF1AN)
TGU: 100224185(HIF1AN)
GFR: 102039688(HIF1AN)
FAB: 101815471(HIF1AN)
PHI: 102110633(HIF1AN)
PMAJ: 107207042(HIF1AN)
CCW: 104697935(HIF1AN)
FPG: 101910571(HIF1AN)
FCH: 102050862(HIF1AN)
CLV: 102094216(HIF1AN)
EGZ: 104129025(HIF1AN)
AAM: 106497781(HIF1AN)
ASN: 102372847(HIF1AN)
AMJ: 102557843(HIF1AN)
PSS: 102461331(HIF1AN)
CMY: 102940361(HIF1AN)
CPIC: 101950170(HIF1AN)
ACS: 100564872(hif1an)
PVT: 110077766(HIF1AN)
PBI: 103049844(HIF1AN)
GJA: 107110489(HIF1AN)
XLA: 108696241(hif1an.L) 432095(hif1an.S)
XTR: 394511(hif1an)
NPR: 108791896(HIF1AN)
DRE: 373126(hif1an)
CCAR: 109056102 109100806(hif1an)
IPU: 100304654(hif1an)
AMEX: 103021617(hif1an)
TRU: 101073285(hif1an)
LCO: 104930472(hif1an)
NCC: 104944324(hif1an)
MZE: 101486879(hif1an)
OLA: 101156274(hif1an)
XMA: 102235402(hif1an)
PRET: 103476845(hif1an)
NFU: 107375913(hif1an)
CSEM: 103387232(hif1an)
LCF: 108880378(hif1an) 108897266
HCQ: 109509915(hif1an)
BPEC: 110173607(hif1an)
ELS: 105021418(hif1an)
SFM: 108925770(hif1an)
LCM: 102346962(HIF1AN)
CMK: 103182440(hif1an)
CIN: 100179426
APLC: 110973644
TCA: 664369(HIF)
NVL: 108569277
DNX: 107173162
ZNE: 110830997
FCD: 110851748
CRG: 105334801
MYI: 110450414
OBI: 106870719
ADF: 107332369
SMIN: v1.2.008839.t1(symbB.v1.2.008839.t1)
 » show all
1  [PMID:11641274]
Mahon PC, Hirota K, Semenza GL
FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity.
Genes. Dev. 15 (2001) 2675-86.
2  [PMID:12042299]
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
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 (2002) 26351-5.
3  [PMID:12432100]
Dann CE 3rd, Bruick RK, Deisenhofer J
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 (2002) 15351-6.
4  [PMID:11823643]
Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML
Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch.
Science. 295 (2002) 858-61.
5  [PMID:14701857]
Koivunen P, Hirsila M, Gunzler V, Kivirikko KI, Myllyharju J
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 (2004) 9899-904.
6  [PMID:12446723]
Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ
Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.
J. Biol. Chem. 278 (2003) 1802-6.
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