Literature summary for 2.5.1.10 extracted from

Rodriguez, J.B.; Falcone, B.N.; Szajnman, S.H.
Approaches for designing new potent inhibitors of farnesyl pyrophosphate synthase (2016), Expert Opin. Drug Discov., 11, 307-320 .

Search for more literature for 2.5.1.10

Inhibitors

Inhibitors	Comment	Organism	Structure
alendronate	-	Homo sapiens
bisphosphonate	-	Homo sapiens
clodronate	-	Homo sapiens
etidronate	-	Homo sapiens
ibandronate	-	Homo sapiens
incadronate	-	Homo sapiens
additional information	the enzyme possesses three inhibition binding sites: the allylic site (dimethyl allyl pyrophosphate and geranyl pyrophosphate), the homoallylic site (isopentenyl pyrophosphate), and the allosteric site. Bisphosphonate-based inhibitors are extremely effective inhibitors binding to the allylic site	Homo sapiens
pamidronate	-	Homo sapiens
Pyrophosphate	-	Homo sapiens
residronate	-	Homo sapiens
tiludronate	-	Homo sapiens
zoledronate	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14324	-	-

General Information

General Information	Comment	Organism
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	Homo sapiens
malfunction	the blockade of farnesyl pyrophosphate synthase prevents the synthesis of farnesyl diphosphate and the downstream essential products	Homo sapiens
metabolism	the enzyme is present in all organisms and constitutes a key enzyme within the mevalonate pathway and the isoprenoid synthesis. It catalyzes the condensation of isopentenyl diphosphate with dimethylallyl diphosphate to give rise to one molecule of geranyl diphosphate, which on a further reaction with another molecule of isopentenyl diphosphate forms the 15-carbon isoprenoid farnesyl diphosphate. This molecule is the obliged precursor for the biosynthesis of sterols, ubiquinones, dolichols, heme A, and prenylated proteins	Homo sapiens

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Release 2023.1 (January 2023)