Myristoylaatioa

Myristoylaatioa refers to the biological process of myristoylation, a type of lipid modification. It involves the covalent attachment of myristic acid, a saturated fatty acid with 14 carbon atoms, to a protein. This attachment typically occurs at the N-terminus of the protein, specifically on an N-terminal glycine residue that is exposed after the removal of the initiator methionine. The reaction is catalyzed by an enzyme called N-myristoyltransferase (NMT).

Myristoylation is considered an irreversible post-translational modification. The myristoyl group is highly hydrophobic, and its attachment significantly alters the physicochemical properties of the protein. This lipid modification can enhance protein-membrane interactions, contributing to the localization of proteins to cellular membranes, such as the plasma membrane or intracellular organelles. It can also play roles in protein folding, stability, and mediating protein-protein interactions. Many cellular proteins, including those involved in signal transduction, cell adhesion, and viral replication, undergo myristoylation. The specific function of myristoylation is context-dependent, varying with the protein and its cellular environment.