After removal of the N-terminal methionine (Met) residue, an unknown N-acyltransferase, similar to the enzymes glycylpeptide N-tetradecanoyltransferase 1 and 2 (NMT1 and 2), mediates the transfer of acyl groups from acyl-CoA to the now N-terminal glycine (Gly) residue of transducin's alpha subunit (GNAT1). The fatty acyl groups transferred are lauroyl (C12:0) and unsaturated myristoyl groups (C14:2 and C14:1). Myristoylation is thought to aid enzyme function and localization. This human event is inferred from bovine experiments demonstrating this activity (Kokame et al 1992).