Members of the ras family of GTP binding proteins, nuclear lamin B, the γ subunit of transducin, and specific yeast mating pheromones are subject to a set of post-translational modifications that culminate in methylation of the α-carboxyl group of a carboxyl-terminal S-farnesylcysteine residue. N-Acetyl-S-trans,trans-farnesyl-l-cysteine (AFC), a small molecule analog of this carboxyl-terminal amino acid, is a substrate of the carboxyl methyltransferase (KM= ∼20 μm). Here we report the synthesis and characterization of AFC and demonstrate how we have exploited its distinctive properties to develop a rapid assay for carboxyl methyltransferase activity.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)