EC Number |
General Information |
Reference |
---|
1.14.11.29 | drug target |
prolyl 4-hydroxylase domain protein 3 (PHD3) overexpression has therapeutic potential in treatment of obstructive sleep apnea and intermittent hypoxia induced cardiovascular fibrosis |
764257 |
1.14.11.29 | evolution |
PHD3 belongs to Fe2+/2-oxoglutarate-dependent oxygenase family |
725644 |
1.14.11.29 | evolution |
the enzyme belongs to the HIF-PHD family of dioxygenases |
745510 |
1.14.11.29 | evolution |
the enzyme belongs to the of the 2-oxoglutarate- and iron-dependent dioxygenase family of enzymes |
724225 |
1.14.11.29 | malfunction |
hypoxia-inducible factor prolyl hydroxylase 2 knockdown leads to a less sustained activation of epidermal growth factor receptor and its downstream signaling pathways |
743380 |
1.14.11.29 | malfunction |
inactivation of Phd2 in endothelial cells specifically results in severe pulmonary hypertension but not polycythemia and is associated with abnormal muscularization of peripheral pulmonary arteries and right ventricular hypertrophy |
743284 |
1.14.11.29 | malfunction |
isoform PHD3 silencing leads to downregulation of most glycolytic enzymes from glucose transport to lactate production supported by the reduction in extracellular acidification and lactate production and increase in cellular oxygen consumption rate |
742225 |
1.14.11.29 | malfunction |
macrophages deficient in PHD3 have decreased levels of stress-induced apoptosis. The antiapoptotic effects of PHD3 knockout are independent of alterations in HIF and instead, appear to occur via reduced expression of Angptl2, an extracellular protein that is structurally similar to angiopoietins. Hypoxia-dependent PHD3 inhibition in macrophages promotes cell survival through the activation of HIF-dependent adaptive pathways and HIF-independent antiapoptotic pathways, including decreased expression of Angptl2, impact of altered PHD3 expression/activity on macrophage function, schematic overview |
745510 |
1.14.11.29 | malfunction |
PHD2 knockdown causes a marked reduction of erythropoietin (EPO) production. HIF seems not to be involved in this process |
744664 |
1.14.11.29 | malfunction |
silencing FIH, EC 1.14.11.30, under conditions where prolyl hydroxylase, is inhibited results in increased HIF-1alpha transcriptional activity, but paradoxically decreases HIF-1alpha stability |
725596 |