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Farnesyl Transferase
- Molecular classification
- Enzyme, Prenyltransferase
01
Overview
Farnesyl transferase (FTase) is an enzyme that catalyzes the posttranslational modification of proteins by attaching a 15-carbon farnesyl isoprenoid group to a cysteine residue near the C-terminus of target proteins. This farnesylation promotes membrane association and proper function of signaling proteins, particularly members of the Ras superfamily. FTase is a heterodimer consisting of alpha and beta subunits, with the active site containing a zinc cation and a hydrophobic pocket for farnesyl diphosphate (FPP) binding. Due to its role in cancer-related Ras protein activation, FTase is an important anti-cancer drug target, with several small-molecule inhibitors developed and tested in clinical trials.
02
Mechanism of action
Inhibition of farnesyl transferase prevents Ras protein membrane localization and downstream signaling.
03
Biological functions
Protein prenylationMembrane targetingSignal transductionCell growthCell differentiation
04
Disease associations
Cancer
05
Safety considerations
Potential for off-target effects due to the involvement of farnesylation in multiple cellular processes.Development of resistance through alternative prenylation pathways (e.g., geranylgeranylation).
06
Interacting drugs
Farnesyl transferase inhibitors
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