NMT2

N-myristoyltransferase 2 (NMT2) is a cytosolic enzyme responsible for the covalent attachment of myristic acid to the N-terminal glycine of target proteins, a critical post-translational modification involved in membrane targeting and protein-protein interactions^[1]. As a paralog of NMT1, NMT2 shares structural similarity but exhibits distinct substrate specificity and tissue expression patterns, suggesting non-redundant roles in cellular regulation^[2]. NMT2 has been implicated in key signaling pathways, including those governing cell proliferation, survival, and apoptosis, particularly in cancer contexts where aberrant lipidation can drive oncogenic transformation^[3]. Recent studies highlight its role in viral infections, such as HIV-1, where NMT2-mediated myristoylation facilitates viral particle assembly and infectivity^[4]. Additionally, emerging evidence links NMT2 dysregulation to neurodegenerative diseases, although its exact contribution remains under investigation^[5]. Unlike NMT1, which is ubiquitously expressed, NMT2 displays more restricted expression, primarily in brain and testis tissues, indicating potential isoform-specific functions^[6]. These distinctions underscore the importance of targeting NMT2 specifically in therapeutic development. Inhibitors selective for NMT2 over NMT1 are being explored as potential anti-cancer and antiviral agents, with early compounds showing promise in preclinical models^[7].