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Literature summary for 1.14.11.30 extracted from

  • Nguyen, L.K.; Cavadas, M.A.; Scholz, C.C.; Fitzpatrick, S.F.; Bruning, U.; Cummins, E.P.; Tambuwala, M.M.; Manresa, M.C.; Kholodenko, B.N.; Taylor, C.T.; Cheong, A.
    A dynamic model of the hypoxia-inducible factor 1alpha (HIF-1alpha) network (2013), J. Cell Sci., 126, 1454-1463.
    View publication on PubMed
Search for more literature for 1.14.11.30

Inhibitors

Inhibitors Comment Organism Structure
additional information temporal dynamics of hydroxylase inhibition, overview Homo sapiens
N-(methoxyoxoacetyl)-glycine methyl ester a pan-hydroxylase inhibitor, in vitro and in vivo inhibition Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 Homo sapiens HIF-1alpha hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293 cell
-
 Homo sapiens
-
Hep-G2 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 HIF-1alpha Homo sapiens hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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 ?

Synonyms

Synonyms Comment Organism
asparaginyl-hydroxylase
-
 Homo sapiens
factor inhibiting HIF
-
 Homo sapiens
FIH
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction silencing FIH under conditions where prolyl hydroxylases, EC 1.14.11.29/30, are inhibited results in increased HIF-1alpha transcriptional activity, but paradoxically decreases HIF-1alpha stability. Residual activity of FIH in hypoxia Homo sapiens
metabolism optimal HIF-1alpha transcriptional activity requires sequential inhibition of both prolyl- and asparaginyl-hydroxylases Homo sapiens
additional information modeling of the dynamic regulation of HIF-1alpha transcriptional activity by the hydroxylase. HIF-1alpha stabilisation and transcriptional activity is dependent on oxygen tension Homo sapiens
physiological function key enzyme in activation of the hypoxia-inducible factor (HIF) pathway, a critical step in the transcriptional response to hypoxia, role of FIH in hydroxylase regulation of HIF-1alpha, overview. The enzyme is involved in the HIF-1alpha signalling network, overview. Asparaginyl hydroxylation confers upon HIF-1alpha resistance to proteosomal degradation, but the removal of the asparaginyl hydroxylation step is necessary for HIF-1alpha activity Homo sapiens