Nmyristoylering

Nmyristoylering is a post-translational modification process in which a myristoyl group, derived from myristic acid, is attached to the amino-terminal glycine residue of a protein. This modification is crucial for the proper folding, stability, and function of certain proteins, particularly those involved in membrane association and signaling. The myristoyl group is attached via an amide bond, forming an N-myristoyl linkage.

The process of Nmyristoylering occurs in the endoplasmic reticulum and is catalyzed by the enzyme N-myristoyltransferase. This enzyme transfers the myristoyl group from myristoyl-CoA to the glycine residue of the protein. The myristoyl group is then often further modified by the addition of a palmitoyl group, a process known as palmitoylation, which enhances the stability and membrane association of the protein.

Nmyristoylering is a reversible process, and the myristoyl group can be removed by specific proteases, such as myristoyl-protein deacylase. This reversible nature allows for the regulation of protein function and localization.

Nmyristoylering is found in a wide range of proteins, including G-proteins, Ras proteins, and certain kinases. It plays a significant role in various cellular processes, such as cell signaling, membrane trafficking, and cell division. Mutations or alterations in the Nmyristoylering process have been linked to several diseases, including cancer and neurodegenerative disorders.