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Ftase

Human protein farnesyltransferase (FTase, EC 2.5.1.58), 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.

References

1.Wang J, et al. Medchemcomm. 2017;8(5):841–854.

Metabolic Enzyme/Protease

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