farnesylotransferaza

Farnesyltransferase, also known as farnesylotransferaza, is an enzyme classified under the EC number 2.5.1.60. It plays a critical role in post-translational modification processes, specifically in the prenylation of certain proteins. This enzyme catalyzes the transfer of a farnesyl group from farnesyl pyrophosphate to a cysteine residue at the C-terminus of target proteins, typically those containing a CaaX motif (where C is cysteine, 'a' is an aliphatic amino acid, and X is any amino acid).

Farnesylation is essential for the proper localization and function of numerous proteins, including members of the Ras superfamily of GTPases, which are involved in cell signaling, growth regulation, and differentiation. The attachment of the farnesyl lipid moiety facilitates the association of these proteins with cellular membranes, which is crucial for their activity within signaling pathways.

Farnesyltransferase consists of a heterodimeric enzyme complex with a catalytic subunit and an accessory subunit, and it functions within the cytoplasm. Its activity has been linked to various biological processes and disease states, notably cancer. Because of this, farnesyltransferase has been a target for drug development, especially in designing inhibitors that can interfere with the prenylation of oncogenic Ras proteins, thereby hindering tumor progression.

Inhibition of farnesyltransferase has shown promise in preclinical and clinical studies for cancer therapy, revealing its potential as a therapeutic target. However, the enzyme also plays roles in normal cellular functions, and ongoing research aims to balance efficacy and safety of farnesyltransferase inhibitors.