NMT1

N-myristoyltransferase 1 (NMT1) is a lipid-modifying enzyme that catalyzes the transfer of myristate to the N-terminal glycine of substrate proteins, thereby regulating protein membrane association, subcellular localization, and signal transduction processes dependent on N-myristoylation^[1][2]. Mechanistically, NMT1 functions during cotranslational protein maturation and promotes efficient modification of nascent proteins after initiator methionine removal, linking protein synthesis to lipid-dependent cellular signaling pathways^[3]. Through regulation of multiple myristoylated signaling proteins, NMT1 influences pathways associated with cell proliferation, survival, and apoptosis, including signaling networks involving Src, focal adhesion kinase, and MAPK cascade components^[4][5]. In disease contexts, elevated dependence on NMT1-mediated myristoylation has been reported in cancer models, where NMT1 supports tumor cell growth and survival through regulation of lysosomal function, autophagic flux, and mTORC1 signaling^[6]. Experimental inhibition of NMT activity impairs lysosomal degradation, disrupts mTORC1 activation, and suppresses tumor growth, supporting the utility of NMT inhibitors as research tools for studying metabolic vulnerabilities in cancer cells^[6]. Compared with the closely related isoform NMT2, NMT1 exhibits partially nonredundant biological functions and is more critical for tumor cell proliferation, despite substantial overlap in substrate processing capacity between the two enzymes^[4][5]. Structural and biochemical studies further demonstrate that NMT1 can catalyze both N-terminal glycine and lysine myristoylation reactions, expanding its functional relevance in protein lipidation research and target validation studies^[7].