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Farnesyltransferase () is one of the three enzymes in the prenyltransferase group. Farnesyltransferase (FTase) adds a 15-carbon isoprenoid called a farnesyl group to proteins bearing a CaaX motif: a four-amino acid sequence at the carboxyl terminus of a protein. Farnesyltransferase's targets include members of the Ras superfamily of small GTP-binding proteins critical to cell cycle progression. For this reason, several FTase inhibitors are undergoing testing as anti-cancer agents. FTase inhibitors have shown efficacy as anti-parasitic agents, as well. FTase is also believed to play an important role in development of progeria and various forms of cancers. Farnesyltransferase catalyzes the chemical reaction :farnesyl diphosphate + protein-cysteine S-farnesyl protein + diphosphate Thus, the two substrates of this enzyme are farnesyl diphosphate and protein-cysteine, whereas its two products are S-farnesyl protein and diphosphate. ==Overview== Farnesyltransferase posttranslationally-modifies proteins by adding an isoprenoid lipid called a farnesyl group to the -SH of the cysteine near the end of target proteins to form a thioether linkage. This process, called farnesylation (which is a type of prenylation), causes farnesylated proteins to become membrane-associated due to the hydrophobic nature of the farnesyl group. Most farnesylated proteins are involved in cellular signaling wherein membrane association is critical for function. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Farnesyltransferase」の詳細全文を読む スポンサード リンク
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