Human protein farnesyltransferase (FTase, EC, one of the three enzymes in the prenyltransferase family, catalyzes the chemical reaction between farnesyl diphosphate and protein-cysteine during the post-translational modifications. Potential FTase substrates include the small GTPase Ras, Rheb, and RhoB, the phosphatases PRL1, 2 and 3, the chaperone protein DnaJ, the cytoplasmic dynein adaptor Spindly, as well as nuclear lamins. These proteins generally contain a CAAX (C = cysteine, A = aliphatic amino acids, and X = a variable amino acid) motif at their carboxyl terminus which can be recognized by FTase. The farnesylation of Ras is the first- and most criticalmodification for the maturing of Ras into its biologically active form, and FTase is of intense interest as a potential tumor therapeutic target. Inhibition of FTase activity can prevent the Ras activation, thereby inhibiting the downstream signaling that related to human tumor initiation and progression.


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