Crystallization (Comment) | Organism |
---|---|
enzyme in complex with peptides of Notch receptor. Significant conformational changes are required in the ankyrin repeat fold of Notch receptor to enable hydroxylation | Mus musculus |
enzyme in complex with peptides of Notch receptor. Significant conformational changes are required in the ankyrin repeat fold of Notch receptor to enable hydroxylation | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ankyrin repeat domain | may function as a natural inhibitor and provide an oxygen-dependent interface that modulates hypoxia-induced factor signaling | Homo sapiens | |
ankyrin repeat domain | may function as a natural inhibitor and provide an oxygen-dependent interface that modulates hypoxia-induced factor signaling | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ankyrin repeat domain of endogenous Notch receptor L-asparagine + 2-oxoglutarate + O2 | hydroxylation of highly conserved asparaginyl residues within the ankyrin repeat | Homo sapiens | ankyrin repeat domain of endogenous Notch receptor 3-hydroxy-L-asparagine + succinate + CO2 | - |
? | |
ankyrin repeat domain of endogenous Notch receptor L-asparagine + 2-oxoglutarate + O2 | hydroxylation of hyghly conserved asparaginyl residues within the ankyrin repeat | Mus musculus | ankyrin repeat domain of endogenous Notch receptor 3-hydroxy-L-asparagine + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
factor inhibiting HIF | - |
Homo sapiens |
HIF asparaginyl hydroxylase | - |
Homo sapiens |