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Literature summary extracted from
- A conserved family of prolyl-4-hydroxylases that modify HIF (2001), Science, 294, 1337-1340.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.11.29 | - |
Homo sapiens |
| 1.14.11.29 | expression in Escherichia coli | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.11.29 | D137A | mutation eliminates prolyl hydroxylase activity of HPH-1 | Homo sapiens |
| 1.14.11.29 | H135A | mutation eliminates prolyl hydroxylase activity of HPH-1 | Homo sapiens |
| 1.14.11.29 | H196A | mutation eliminates prolyl hydroxylase activity of HPH-1 | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.11.29 | oxygen | the transiently overexpressed HPH-1 enzyme is inhibited by a low-oxygen environment | Homo sapiens |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.11.29 | Fe2+ | the enzyme contains Fe2+ | Homo sapiens | |
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 | Homo sapiens | mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl hydroxylase is responsible for this posttranslational modification | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
| 1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | Homo sapiens | mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl is responsible for this posttranslational modification | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.11.29 | Drosophila melanogaster | - |
- |
- |
| 1.14.11.29 | Homo sapiens | - |
- |
- |
| 1.14.11.29 | Homo sapiens | Q96KS0 | HPH-3 | - |
| 1.14.11.29 | Homo sapiens | Q9GZT9 | HPH-2 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.11.29 | - |
Homo sapiens |
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 | mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl hydroxylase is responsible for this posttranslational modification | Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
| 1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl is responsible for this posttranslational modification | Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
| 1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified | Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
| 1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified. The endogenous HIF prolyl hydroxylase, HPH-1 generates by in vitro transcription/translation does not modify peptides containing the L562A, A563G, or Y565A mutations. However, a peptide containing the Pro567 to Gly mutation is an equal, if not better, substrate for the human HPH enzymes | Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
| 1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified. The recombinant HPH-2 purified from Escherichia coli does not modify peptides containing the L562A, A563G, or Y565A mutations. However, a peptide containing the Pro567 to Gly mutation is an equal, if not better, substrate for the human HPH enzymes | Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.11.29 | HIF prolyl | - |
Homo sapiens |
| 1.14.11.29 | HIF prolyl hydroxylase | - |
Drosophila melanogaster |
| 1.14.11.29 | HIF prolyl hydroxylase | - |
Homo sapiens |
| 1.14.11.29 | HPH-1 | - |
Homo sapiens |
| 1.14.11.29 | HPH-2 | - |
Homo sapiens |
| 1.14.11.29 | HPH-3 | - |
Homo sapiens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.11.29 | physiological function | in cultured mammalian cells, inappropriate accumulation of hypoxia-inducible factor caused by forced expression of the hypoxia-inducible factor-1alpha subunit under normoxic conditions is attenuated by coexpression of HIF prolyl hydroxylase. Suppression of HIF prolyl hydroxylase in cultured Drosophila melanogaster cells by RNA interference results in elevated expression of a hypoxia-inducible gene (LDH, encoding lactate dehydrogenase) under normoxic conditions. HIF prolyl hydroxylase is an essential component of the pathway through which cells sense oxygen | Homo sapiens |
| 1.14.11.29 | physiological function | in cultured mammalian cells, inappropriate accumulation of hypoxia-inducible factor caused by forced expression of the hypoxia-inducible factor-1alpha subunit under normoxic conditions is attenuated by coexpression of HIF prolyl. Suppression of HIF prolyl in cultured Drosophila melanogaster cells by RNA interference results in elevated expression of a hypoxia-inducible gene (LDH, encoding lactate dehydrogenase) under normoxic conditions. HIF prolyl is an essential component of the pathway through which cells sense oxygen | Homo sapiens |
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