Prenylation is the covalent attachment of an isoprenyl group to a protein, and is one of the most common post-translational modifications. In mammals, up to 2% of cellular proteins undergo prenylation. These modifications mediate both protein-membrane and protein–protein interactions.

Prenylation is the first reaction in a three‐step maturation process that involves initial attachment of the prenyl group to a specific cysteine residue present near the C‐terminus of a protein via the formation of a thioether bond. This reaction is catalyzed by a class of enzymes called protein prenyl transferases that use either farnesyl ...

These characteristic features of TleC and MpnD make the enzymes excellent targets for the manipulation of the prenylation reactions. The structure-based engineering of TleC and MpnD...

Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or a biomolecule. It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed.

Tandem mass spectrometry, when combined with micro-HPLC, provides a method for characterizing the entire C-terminal structure of the protein of interest (prenylation, proteolysis, and methylation). Because of mass speciation, this method is useful for analyzing complex mixtures such as tryptic digests of native proteins.