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Literature summary extracted from

  • Wang, L.; Cui, S.; Ma, L.; Kong, L.; Geng, X.
    Current advances in the novel functions of hypoxia-inducible factor and prolyl hydroxylase in invertebrates (2015), Insect Mol. Biol., 24, 634-648 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 Drosophila melanogaster hypoxia-inducible factor 1alpha is hydroxylated at Pro402 and Pro564 hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
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1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 Caenorhabditis elegans hypoxia-inducible factor 1alpha is hydroxylated at Pro402 and Pro564 hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
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Organism

EC Number Organism UniProt Comment Textmining
1.14.11.29 Caenorhabditis elegans
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-
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1.14.11.29 Drosophila melanogaster
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor 1alpha is hydroxylated at Pro402 and Pro564 Drosophila melanogaster hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
-
?
1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor 1alpha is hydroxylated at Pro402 and Pro564 Caenorhabditis elegans hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
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?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.29 hydroxylase domain enzyme
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Drosophila melanogaster
1.14.11.29 hydroxylase domain enzyme
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Caenorhabditis elegans
1.14.11.29 PHD
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Drosophila melanogaster
1.14.11.29 PHD
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Caenorhabditis elegans
1.14.11.29 prolyl 4-hydroxylase
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Drosophila melanogaster
1.14.11.29 prolyl 4-hydroxylase
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Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
1.14.11.29 metabolism isoforms PHD2 and 3 inhibit IkappaB kinase and decrease the activity of the nuclear factor-kappaB pathway. Isoform PHD2 also acts as a negative regulator of nuclear factor-kappaB during arteriogenesis Drosophila melanogaster
1.14.11.29 metabolism isoforms PHD2 and 3 inhibit IkappaB kinase and decrease the activityof the nuclear factor-kappaB pathway. Isoform PHD2 also acts as a negative regulator of nuclear factor-kappaB during arteriogenesis Caenorhabditis elegans