NMT2 (N-myristoyltransferase 2) is a ubiquitously expressed enzyme that catalyzes the addition of myristic acid to N-terminal glycine residues of nascent proteins 1, and can also mediate N-terminal lysine myristoylation as demonstrated with ARF6 substrate 2. This lipid modification is essential for membrane targeting and protein function. Mechanistically, NMT2 couples to protein synthesis through interaction with the nascent polypeptide-associated complex (NAC), which mediates NMT2 binding to translating ribosomes and orients the enzyme for co-translational myristoylation 3. NMT2 activity is regulated by NADPH, which upregulates myristoylation of ferroptosis suppressor protein 1 (FSP1), strengthening cellular resistance to ferroptosis in neurons 4. Clinically, NMT2 dysregulation is significant in cancer: epigenetic suppression of NMT2 in hematologic malignancies renders cells dependent on NMT1, making them vulnerable to NMT inhibitors that selectively target mitochondrial oxidative phosphorylation 5. Conversely, low NMT2 expression associates with poor prognosis in non-small cell lung cancer, where NMT1/NMT2 function as tumor suppressors 6. Additionally, NMT2 is required for mammarenavirus replication, as the Z matrix protein and signal peptide depend on myristoylation for viral budding and entry; NMT inhibitors demonstrate broad-spectrum antiviral activity against Lassa and other hemorrhagic fever viruses 78.