Recombinant NMT1 protein (His tag)

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This product is a high-quality recombinant fragment of Human Glycylpeptide N-tetradecanoyltransferase 1 (NMT1), spanning residues 105-496. This stable and soluble fragment is ideal for structural studies, enzymatic assays, and investigating the mechanisms of protein N-myristoylation and lysine myristoylation.

Glycylpeptide N-tetradecanoyltransferase 1 (NMT1) is a crucial enzyme that catalyzes the addition of a myristoyl group to the N-terminal glycine residue of various cellular and viral proteins, a modification essential for protein-membrane interactions and signaling. Notably, it also mediates N-terminal lysine myristoylation, as demonstrated with ARF6, which is required to maintain ARF6 on membranes during its GTPase cycle. The full-length protein is primarily localized in the cytoplasm and cytosol and can associate with membranes as a peripheral membrane protein. It has been observed to copurify with ribosomes, indicating potential roles in coordinating protein lipid modification with translation or ribosomal function. This fragment represents a computationally selected stable unit, enabling detailed biochemical and structural exploration of NMT1's catalytic activity and regulatory mechanisms.