ABSTRACT
The chemical structure of isoprenoids consisting of multiple units of five carbon atoms and their biosynthesis derived from the consecutive condensation of single precursors: the monomer isopentenyl diphosphate and its isomer DMAPP. Protein prenylation, in particular farnesylation and geranylgeranylation, is one of the essential post-translational protein modifications in the eukaryote in which protein prenyltransferases catalyze the transfer of farnesyl pyrophosphate synthase or geranylgeranyl pyrophosphate synthase to cysteine residues located in conserved prenylation target motifs at the C-terminus of the protein substrate. The presence of nitrogen on the substituents results in nitrogen-containing-bisphophonates, while the absence of nitrogen leads to non-nitrogen-containing-bisphophonates. The methanesulfonic acid allows the reaction to remain fluid, obtaining complete conversion and high yields, even with substrates bearing amino functionality. Carboxylic acids activated as acyloxybenzodioxaborolane intermediates were proposed as an alternative to the acid chlorides.
