EC Number   |
General Information |
Reference |
|---|
    2.5.1.10 | drug target |
antimalarial drug target |
759015 |
| 2.5.1.10 | drug target |
due to its crucial role in isoprenoid biosynthesis, the enzyme is a molecular target for the treatment of different bone disorders and to control parasitic diseases, particularly, those produced by trypanosomatids and Apicomplexan parasites. Notwithstanding their lack of drug-like character, bisphosphonates are the most advantageous class of inhibitors of the enzymatic activity of farnesyl pyrophosphate synthase. The poor drug-like character is largely compensated by the high affinity of the bisphosphonate moiety by bone mineral hydroxyapatite in humans. Several bisphosphonates are currently in use for the treatment of a variety of bone disorders. Currently, the great prospects that bisphosphonates behave as antiparasitic agents is due to their accumulation in acidocalcisomes, organelles with equivalent composition to bone mineral, hence facilitating their antiparasitic action |
759159 |
| 2.5.1.10 | drug target |
farnesyl diphosphate synthase is in a branching point in sterol metabolic pathways. It is a key enzyme in the mevalonate pathway and a good candidate for drug design |
-, 759898 |
| 2.5.1.10 | drug target |
the enzyme is a drug target for the treatment of cutaneous leishmaniasis |
-, 759751 |
| 2.5.1.10 | drug target |
the enzyme is a target for treating bone resorption diseases and some cancers |
759609 |
| 2.5.1.10 | drug target |
the enzyme plays a significant role in the disease-related cell signaling pathway, and the inhibition of the enzyme is a potential approach for treating FPPS-regulated diseases |
759151 |
| 2.5.1.10 | drug target |
Trypanosoma brucei is the causative agent of human African trypanosomiasis. Nitrogen-containing bisphosphonates, a current treatment for bone diseases, have been shown to block the growth of the Trypanosoma brucei parasites by inhibiting farnesyl pyrophosphate synthase. However, due to their poor pharmacokinetic properties, they are not well suited for antiparasitic therapy. Tthe discovery of new binding sites and non-bisphosphonate binders is a critical step towards the investigation of farnesyl pyrophosphate synthase as a drug target for human African trypanosomiasis and opens up the possibility of a fragment-to-lead optimisation program |
759064 |
| 2.5.1.10 | evolution |
Giardia and Leishmania farnesyl diphosphate synthase enzymes are phylogenetically distant but display conserved protein signatures. The nitrogen-containing bisphosphonates effect on farnesyl diphosphate synthase is more pronounced in Leishmania than Giardia. This might be due to general differences in metabolism and differences in the farnesyl diphosphate synthase catalytic site |
-, 759898 |
| 2.5.1.10 | evolution |
reported of the molecular evolution of positive selection sites in plant. Gene expression analysis shows that FPS genes could increase terpenoid accumulation in plants. Large-scale evolutionary analysis of farnesyl diphosphate synthase in land plants. It explores the relationship between the molecular evolution of positive selection sites and their roles in plant farnesyl diphosphate synthase. Farnesyl diphosphate synthase genes in plants appeared very early, and can be traced back to the bryophyte divergence to pteridophyte, which then evolves into gymnospermae, monocotyledonae, and dicotyledoneae. A number of signals for positive selection exist in plant farnesyl diphosphate synthases. Thirty-nine positively selected sites in the site model and three positively selected sites in the branch-site model are detected, respectively |
758971 |
| 2.5.1.10 | evolution |
reported of the molecular evolution of positive selection sites in plant. Gene expression analysis shows that FPS genes could increase terpenoid accumulation in plants. Large-scale evolutionary analysis of farnesyl diphosphate synthase in land plants. It explores the relationship between the molecular evolution of positive selection sites and their roles in plant farnesyl diphosphate synthase. Farnesyl diphosphate synthase genes in plants appeared very early, and can be traced back to the bryophyte divergence to pteridophyte, which then evolves into gymnospermae, monocotyledonae, and dicotyledoneae. A number of signals for positive selection exist in plant farnesyl diphosphate synthases. Thirtynine positively selected sites in the site model and three positively selected sites in the branch-site model are detected, respectively |
758971 |
