EC Number   |
Natural Substrates |
|---|
   1.14.11.2 | (Gly-Pro-Pro)10 + 2-oxoglutarate + O2 |
- |
| 1.14.11.2 | Argonaute 2 + 2-oxoglutarate + O2 |
regulation of Ago 2 protein activity via substrate protein stability involving Ago Pro700 residue, the Ago protein mutant P700A is destabilized, overview |
| 1.14.11.2 | hypoxia-inducible factor L-proline + 2-oxoglutarate + O2 |
- |
| 1.14.11.2 | hypoxia-inducible transcription factor + 2-oxoglutarate + O2 |
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview |
| 1.14.11.2 | hypoxia-inducible transcription factor + 2-oxoglutarate + O2 |
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview |
| 1.14.11.2 | hypoxia-inducible transcription factor + 2-oxoglutarate + O2 |
i.e. HIF, oxygen-dependent hydroxylation of proline residues in the alpha subunit of hypoxia-inducible transcription factor is central to the hypoxic response in animals. Prolyl hydroxylation of HIFalpha increases its binding to the von Hippel-Lindau protein, thus signaling for degradation via the ubiquitin-proteasome system |
| 1.14.11.2 | more |
molecular mechanism of intracellular degradation of type I collagen in normal corneal endothelial cells, role of the enzyme and protein-disulfide isomerase, which is the beta subunit of the enzyme, during procollagen I biosynthesis |
| 1.14.11.2 | more |
HPH isoforms are involved in infection of hosts and stress response |
| 1.14.11.2 | more |
HIF prolyl hydroxylases are related to the collagen prolyl hydroxylases, but form unusually stable complexes with their Fe2+ cofactor and 2-oxoglutarate cosubstrate |
| 1.14.11.2 | more |
the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2 |
