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Literature summary for 1.14.11.29 extracted from

  • Cavadas, M.A.; Nguyen, L.K.; Cheong, A.
    Hypoxia-inducible factor (HIF) network: insights from mathematical models (2013), Cell Commun. Signal., 11, 42.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 Homo sapiens PHD enzymes hydroxylates HIF-alpha at prolyl residues present in the transcriptional activation domain N-TAD hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
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Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2
-
Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 PHD enzymes hydroxylates HIF-alpha at prolyl residues present in the transcriptional activation domain N-TAD Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
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?

Synonyms

Synonyms Comment Organism
PHD
-
Homo sapiens
PHD2
-
Homo sapiens
PHD3
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Homo sapiens
prolyl hydroxylase domain
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Homo sapiens

General Information

General Information Comment Organism
metabolism HIF protein stability is controlled by the oxygen sensing prolyl hydroxylase domain enzymes. Hypoxia-induced HIF signalling, mathematical modelling of the pathway, temporal dynamics of the HIF response to hypoxia, and molecular interaction map for the HIF network, overview. The hypoxia inducible factor is switched on and promotes adaptation to hypoxia by upregulatinggenes involved in angiogenesis, erythropoiesis and glycolysis Homo sapiens
additional information PHD has a higher affinity for oxygen than FIH, EC 1.14.11.30 Homo sapiens
physiological function HIF transcriptional activity is controlled by the asparaginyl hydroxylase factor inhibiting HIF-1, FIH Homo sapiens