EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.29 | ascorbate | enhances activity | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.29 | N-oxalyl-(2S)-alanine | competed by 2-oxoglutarate, no inhibition by the enantiomer N-oxalyl-(2R)-alanine | Homo sapiens | |
1.14.11.29 | N-oxalylglycine | competed by 2-oxoglutarate | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.11.29 | Fe2+ | required. the enzyme activity is inhibited by substitution of Fe2+ with Co2+ or Ni2+ | Homo sapiens |
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 | hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. The interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by HIF-alpha prolyl-hydroxylase (HIF-PH). HIF-PH functions directly as a cellular oxygen sensor | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.11.29 | Homo sapiens | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | - |
Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? | |
1.14.11.29 | hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 | hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. The interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by HIF-alpha prolyl-hydroxylase (HIF-PH). HIF-PH functions directly as a cellular oxygen sensor | Homo sapiens | hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.11.29 | HIF-alpha prolyl-hydroxylase | - |
Homo sapiens |
1.14.11.29 | HIF-PH | - |
Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.11.29 | physiological function | hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. The interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by HIF-alpha prolyl-hydroxylase (HIF-PH). HIF-PH functions directly as a cellular oxygen sensor. Exposure of cells to dimethyl-oxalylglycine, that penetrates cells readily, results in rapid induction of HIF-1alpha | Homo sapiens |