Acylation at the N-terminus is a common modification in natural proteins. [3] [4] [5] [6] Myristic acid (Myr-OH) or other longchain fatty acids, such as lauric acid (Lau-OH) 7-10) and palmitic acid (Pal-OH), 11) in rare cases, are found in amide linkage with the N-terminal Gly residue of proteins. The acylation by Myr-OH is catalyzed by N-myristoyl transferases, which have been identified and characterized. These enzymes catalyze transfer of Myr specifically to the N-terminal Gly of proteins,

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... d require the consensus sequence Gly-X-X-X-Acylation with long-chain fatty acids is a common modification at the N-terminal glycine residues of natural proteins. In this work, we performed HPLC analysis of myristoylglycine (Myr-Gly-OH), palmitoylglycine (Pal-Gly-OH) or lauroylglycine (Lau-Gly-OH), which were produced in the hydrolysates of synthetic Myr-Gly-, Pal-Gly-, or Lau-Gly-peptides, respectively, by means of a mild acid hydrolysis in methanesulfonic acid : dioxane : water (2 : 1 : 1) at 60°C for 12 h. Myr-Gly-OH, Pal-Gly-OH and Lau-Gly-OH were quite stable under hydrolysis conditions. These fatty acyl-Gly-OH were conveniently detectable at a 20 nmol level by direct reversed-phase HPLC. Thus, mild acid hydrolysis, followed by HPLC analysis of the hydrolysate, provides a simple method of identification of the N-terminal structure of fatty acyl-Gly-peptides.