Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product. [PDF]
Abstract Farnesyl pyrophosphate synthase (FPPS) is an enzyme of the mevalonate pathway and a well-established therapeutic target. Recent research has focused around a newly identified druggable pocket near the enzyme’s active site.
Park J +4 more
europepmc +5 more sources
Inhibition of human mevalonate kinase by allosteric inhibitors of farnesyl pyrophosphate synthase. [PDF]
Mevalonate kinase is a key regulator of the mevalonate pathway, subject to feedback inhibition by the downstream metabolite farnesyl pyrophosphate. In this study, we validated the hypothesis that monophosphonate compounds mimicking farnesyl pyrophosphate can inhibit mevalonate kinase.
Salari S, Lee HF, Tsantrizos YS, Park J.
europepmc +4 more sources
Molecular Cloning and Characterisation of Farnesyl Pyrophosphate Synthase from Tripterygium wilfordii. [PDF]
Farnesylpyrophosphate synthase (FPS) catalyzes the biosynthesis of farnesyl pyrophosphate (FPP), which is an important precursor of sesquiterpenoids such as artemisinin and wilfordine. In the present study, we report the molecular cloning and characterization of two full-length cDNAs encoding FPSs from Tripterygium wilfordii (TwFPSs). TwFPSs maintained
Zhao YJ +8 more
europepmc +6 more sources
Inhibition of farnesyl pyrophosphate synthase alleviates cardiomyopathy in diabetic rat. [PDF]
This study investigated the effects of ibandronate (IBN) on cardiomyopathy remodeling in diabetic rats. A rat model of diabetic cardiomyopathy (DCM) was established by supplementing them with a high-calorie diet combined with a low dose of streptozotocin (STZ).
Liu X, Liu Y, Tang L, Du C.
europepmc +3 more sources
Strengthening Triterpene Saponins Biosynthesis by Over-Expression of Farnesyl Pyrophosphate Synthase Gene and RNA Interference of Cycloartenol Synthase Gene in Panax notoginseng Cells [PDF]
To conform to the multiple regulations of triterpene biosynthesis, the gene encoding farnesyl pyrophosphate synthase (FPS) was transformed into Panax notoginseng (P.
Diqiu Liu, Feng Ge, Liu Diqiu
exaly +4 more sources
Farnesyl pyrophosphate synthase is essential for the promastigote and amastigote stages in Leishmania major. [PDF]
Isoprenoid synthesis provides a diverse class of biomolecules including sterols, dolichols, ubiquinones and prenyl groups. The enzyme farnesyl pyrophosphate synthase (FPPS) catalyzes the formation of farnesyl pyrophosphate, a key intermediate for the biosynthesis of all isoprenoids.
Mukherjee S, Basu S, Zhang K.
europepmc +4 more sources
Positive selection and functional divergence of farnesyl pyrophosphate synthase genes in plants. [PDF]
Farnesyl pyrophosphate synthase (FPS) belongs to the short-chain prenyltransferase family, and it performs a conserved and essential role in the terpenoid biosynthesis pathway. However, its classification, evolutionary history, and the forces driving the evolution of FPS genes in plants remain poorly understood.Phylogeny and positive selection analysis
Qian J +6 more
europepmc +4 more sources
Lentiviral-mediated silencing of farnesyl pyrophosphate synthase through RNA interference in mice. [PDF]
Farnesyl pyrophosphate synthase (FPPS) plays a vital role in the mevalonate pathway and has been shown to be involved in hypertrophy and cardiovascular diseases. Lentivirus-mediated RNA interference (RNAi) to knock down a gene of interest has become a promising new tool for the establishment of transgenic animals.
Yang J +5 more
europepmc +4 more sources
Enzymatic Prenylation of Proteins and Peptides: From Cysteine S-Prenylation to Tryptophan-Selective Biocatalysis. [PDF]
This review highlights biocatalytic prenylation as a versatile strategy for tailoring the functional properties of peptides and proteins. By comparing branched isoprenoids with linear lipids, we illustrate how specific prenyl architectures modulate the behaviors of lipidated proteins within membrane environments.
Fujinami D, Ozawa H, Ito S.
europepmc +2 more sources
Farnesyl pyrophosphate synthase promotes restenosis after vascular injury by activating small G proteins [PDF]
Yajun Liu
exaly +2 more sources

