1.14.11.30: hypoxia-inducible factor-asparagine dioxygenase
This is an abbreviated version!
For detailed information about hypoxia-inducible factor-asparagine dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.30
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1.14.11.30
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prolyl
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hydroxylases
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transactivation
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oxygen-dependent
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ankyrin
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normoxia
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hippel-lindau
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oxygen-sensing
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hif-alpha
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prolyl-hydroxylase
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fih-mediated
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2og-dependent
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hypoxia-sensitive
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dimethyloxalylglycine
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2-oxoglutarate-dependent
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medicine
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drug development
- 1.14.11.30
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prolyl
- hydroxylases
-
transactivation
-
oxygen-dependent
- ankyrin
-
normoxia
-
hippel-lindau
-
oxygen-sensing
-
hif-alpha
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prolyl-hydroxylase
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fih-mediated
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2og-dependent
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hypoxia-sensitive
- dimethyloxalylglycine
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2-oxoglutarate-dependent
- medicine
- drug development
Reaction
Synonyms
asparaginyl hydroxylase, asparaginyl-hydroxylase, factor inhibiting HIF, factor inhibiting HIF-1, factor inhibiting hypoxia inducible factor-1alpha, factor-inhibiting HIF, factor-inhibiting hypoxia inducible factor, factor-inhibiting hypoxia-inducible factor, FIH, FIH hydroxylase, HIF asparagine hydroxylase, HIF asparaginyl hydroxylase, HIF hydroxylase, HIF1AN, hypoxia-inducible factor 1-alpha inhibitor, hypoxia-inducible factor asparagine hydroxylase
ECTree
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Natural Substrates Products on EC 1.14.11.30 - hypoxia-inducible factor-asparagine dioxygenase
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REACTION DIAGRAM
hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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activity of the hypoxia-inducible factor (HIF) complex is controlled by oxygen-dependent hydroxylation of prolyl and asparaginyl residues. Hydroxylation of specific prolyl residues by 2-oxoglutarate-dependent oxygenases mediates ubiquitinylation and proteasomal destruction of HIF-alpha. Hydroxylation of an asparagine residue (ASn803) in the C-terminal transactivation domain of HIF-alpha abrogates interaction with p300, preventing transcriptional activation
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hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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the activity of hypoxia-inducible transcription factor HIF, an alphabeta heterodimer that has an essential role in adaptation to low oxygen availability, is regulated by two oxygen-dependent hydroxylation events. Hydroxylation of specific proline residues by HIF prolyl 4-hydroxylases targets the HIF-alpha subunit for proteasomal destruction, whereas hydroxylation of an asparagine in the C-terminal transactivation domain prevents its interaction with the transcriptional coactivator p300
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hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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FIH hydroxylates Asn803 of HIF-1alpha
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hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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FIH hydroxylates at the asparaginyl residue in the FIH transcriptional activation domain C-TAD
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hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
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HIF-1alpha
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hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2
hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2
hydroxylation at Asn803
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