Function
Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Biological Context
Subcellular Location: Cytoplasm
Disease Association: Porokeratosis 9, multiple types (POROK9) : A form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported. [The disease is caused by variants affecting the gene represented in this entry]
Pathway: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1
Product Specifications
Recombinant Human Farnesyl pyrophosphate synthase (FDPS) is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 1-419aa, with N-terminal 6xHis-SUMO-tagged tag, molecular weight 64.3kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Enzyme proteins →
