FDPS
FDPS (farnesyl diphosphate synthase) is a key cytoplasmic enzyme in isoprenoid biosynthesis. It catalyses the formation of farnesyl pyrophosphate (FPP), a precursor for sterols, dolichols, carotenoids and ubiquinones, and a substrate for protein prenylation. Browse Assay Genie's current range of FDPS research reagents below, or read on for the biology behind the target.
FDPS is a key enzyme in isoprenoid biosynthesis. It catalyses the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates: first dimethylallyl pyrophosphate, and then the resulting geranyl pyrophosphate, to give the final product, farnesyl pyrophosphate (FPP). FPP is a precursor for several classes of essential metabolites, including sterols, dolichols, carotenoids and ubiquinones.
FPP also serves as a substrate for protein farnesylation and geranylgeranylation. According to the NCBI Gene summary, it is a key intermediate in cholesterol and sterol biosynthesis, and a ligand or agonist for certain hormone receptors and growth receptors. The enzyme is found in the cytoplasm and belongs to the FPP/GGPP synthase family. The human FDPS gene has mouse and rat orthologs, both named Fdps.
Drugs that inhibit this enzyme prevent the post-translational modification of small GTPases and have been used to treat diseases related to bone resorption, which makes FDPS a well-established pharmacological target. The genome also contains multiple pseudogenes on chromosomes 1, 7, 14, 15, 21 and X, and multiple transcript variants encoding different isoforms have been described. These features are worth considering when designing experiments to study the FDPS protein and its expression.
FDPS produces FPP, a precursor for sterols, dolichols, carotenoids and ubiquinones, placing it at a central branch point of isoprenoid biosynthesis.
FPP is a key intermediate in cholesterol and sterol biosynthesis, so FDPS is relevant to studies of this pathway.
FPP is the substrate for protein farnesylation and geranylgeranylation, and FDPS inhibition prevents post-translational modification of small GTPases.
Inhibitors of FDPS have been used to treat diseases related to bone resorption, making the enzyme a focus for drug mechanism studies.
FDPS catalyses the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate and then geranyl pyrophosphate, producing farnesyl pyrophosphate. This product feeds sterol, dolichol, carotenoid and ubiquinone synthesis, and is a substrate for protein farnesylation and geranylgeranylation.
The official name is farnesyl diphosphate synthase, and UniProt lists the protein as farnesyl pyrophosphate synthase. No alternative gene symbols are recorded by HGNC. NCBI Gene reports multiple transcript variants encoding different isoforms, along with several pseudogenes on other chromosomes.
Mouse and rat both have an ortholog named Fdps. Disease relevance comes mainly through pharmacology: drugs that inhibit this enzyme block post-translational modification of small GTPases and are used for diseases of bone resorption. Check the datasheet of any product for its validated reactivity.
Other isoprenoid and cholesterol biosynthesis enzymes and protein prenylation targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P14324; product specifications from Assay Genie datasheets.