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N-myristoylation demonstrates diverse cellular functions in eukaryotes, suggesting important roles in proteins and trafficking.
Protein N-myristoylation refers to the covalent attachment of myristic acid, a 14-carbon saturated fatty acid (C14:0), to the N-terminal glycine of proteins. Linkage occurs via an amide bond and takes place as proteins are being synthesized. N-myristoylproteins have varied intracellular destinations, and are involved in myriad cellular functions ranging from signal transduction to protein and vesicular trafficking. N-myristoylproteins are encountered in members of all kingdoms of the eukaryotic domain (Protist, Fungi, Plant, and Animal), but are not produced by members of Bacteria or Archaea. MyristoylCoA: protein N-myristoyltransferase (Nmt), E.C. 2.3.1.97, a member of the GCN5 acetyltransferase (GNAT) superfamily, is responsible for catalyzing the transfer of myristate from myristoylCoA to proteins. While the acylCoA substrate specificity of Nmt has been highly conserved during evolution, its peptide substrate specificities have diverged among eukaryotes.
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Gordon et al. (1991) studied this question.
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