Fig. 5

The catalytic mechanism and process of protein N-myristoylation. a Cotranslational myristoylation usually occurs on the glycine at the N-terminal end of nascent proteins after the methionine initiator has been removed by MetAP2. The catalytic mechanism follows the Bi–Bi mechanism. Conformational changes were induced after NMTs bound to the fatty acid chain of the myristoyl-CoA binding site. Then, the substrate binds to the NMTs and produces myristoylpeptide via a myristoyl transfer reaction. Finally, the NMTs release the myristoylpeptide and restore its conformation. b Posttranslational protein N-myristoylation often occurs during apoptosis. After the internal glycine of the substrate protein is exposed by caspase cleavage, NMTs catalyse the attachment of myristic acid to the glycine residue of the substrate. c Reversible protein N-myrisotylation occurs on the Nε-side chain of lysine residues instead of glycine residues, which is reversed by sirtuins or HDACs