| farnesyl-diphosphate farnesyltransferase 1 | |
|---|---|
| Identifiers | |
| Symbol | FDFT1 |
| Entrez | 2222 |
| HUGO | 3629 |
| OMIM | 184420 |
| RefSeq | NM_004462 |
| UniProt | P37268 |
| Other data | |
| EC number | 2.5.1.21 |
| Locus | Chr. 8 p23.1-p22 |
Farnesyl-diphosphate farnesyltransferase (FDFT1) (or squalene synthase (SQS)) is an enzyme that converts two units of farnesyl pyrophosphate into squalene.
It has been described as the first dedicated enzyme of sterol (i.e., cholesterol, etc.) synthesis, since the squalene formed by it is exclusively routed into various sterols via a complex, multi-step pathway.
Contents |
Squalene synthase is considered to be an enzyme of eukaryotes or advanced organisms, although at least one prokaryote has been shown to possess a functionally similar enzyme.
In terms of structure and mechanics, squalene synthase most closely resembles phytoene synthase, which serves a similar role in many plants in the elaboration of phytoene, a precursor of many carotenoid compounds. (Carotenoids are the colorful pigments present in most vegetables.)
Click on genes, proteins and metabolites below to link to respective articles. [1]
Inhibition of squalene synthase, e.g., by lapaquistat, is under investigation as a method of lowering cholesterol levels in the prevention of cardiovascular disease.[2][3] It has also been suggested that variants in this enzyme may be part of a genetic association with hypercholesterolemia.[4] (Lapaquistat is no longer being investigated for clinical use.)
Other squalene synthase inhibitors include Zaragozic acid, and RPR 107393[5].
Squalene synthase homolog inhibition in Staphylococcus aureus is currently being investigated as a virulence factor-based antibacterial therapy. [6]
|
||||||||
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||