The vast majority of eukaryotic proteins are N‐terminally modified by one or more
processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include …

Protein N-myristoylation is a cotranslational lipidic modification specific to the alpha-amino
group of an N-terminal glycine residue of many eukaryotic and viral proteins. The ubiquitous …

Myristoylation corresponds to the irreversible covalent linkage of the 14-carbon saturated
fatty acid, myristic acid, to the N-terminal glycine of many eukaryotic and viral proteins. It is …

Co-translational modification of eukaryotic proteins by N-myristoylation aids subcellular
targeting and protein-protein interactions. The enzyme that catalyzes this process, N …

Colorectal cancer is the second leading cause of malignant death, and better preventive
strategies are needed. The treatment of colonic cancer remains difficult because of the lack …

N-myristoyl transferase (NMT) catalyzes the transfer of the fatty acid myristate from myristoyl-
CoA to the N-terminal glycine of substrate proteins, and is found only in eukaryotic cells. The …

Infections caused by protozoan parasites are among the most widespread and intractable
transmissible diseases affecting the developing world, with malaria and leishmaniasis being …

N-Myristoyltransferase (NMT) catalyzes the cotranslational acylation with myristic acid of the
NH 2-terminal glycines of a number of cellular and viral proteins. Most of the in vitro NMT …

Myristoylation refers to the co-translational addition of a myristoyl group to an amino-terminal
glycine residue of a protein by an ubiquitously distributed enzyme myristoyl-CoA: protein N …

The eukaryotic enzyme NMT (myristoyl-CoA: protein N-myristoyltransferase) has been
characterized in a range of species from Saccharomyces cerevisiae to Homo sapiens. NMT …