dodecanoylation

Dodecanoylation is a biochemical process that involves the attachment of a dodecanoyl group, which is a twelve-carbon fatty acid chain, to a protein or other biomolecule. This modification is a type of lipidation, where a lipid molecule is covalently attached to a protein. Dodecanoylation can occur on various amino acid residues, most commonly on cysteine, but also on serine, threonine, or lysine residues. The dodecanoyl group is typically derived from lauric acid, a saturated fatty acid.

This process is often mediated by specific enzymes. For instance, acyltransferases can catalyze the transfer of the dodecanoyl moiety from a donor molecule, such as dodecanoyl-CoA, to the target biomolecule. The resulting dodecanoylated molecule can exhibit altered properties compared to its unmodified form. These changes can include increased hydrophobicity, which can affect its solubility, membrane association, and interactions with other molecules.

Dodecanoylation plays a role in various biological functions. It has been observed in the modification of certain signaling molecules, enzymes, and structural proteins. The attachment of the dodecanoyl chain can influence protein localization, stability, and activity. While less extensively studied than some other lipidation events, dodecanoylation represents an important post-translational modification that contributes to the complexity and regulation of cellular processes. Research into dodecanoylation continues to uncover its specific roles in different biological systems.