NMT1 Human
Greater than 85.0% as determined by SDS-PAGE.
Description
NMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
N-Myristoyltransferase 1 (NMT1) is an essential enzyme that catalyzes the covalent attachment of myristic acid, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of substrate proteins. This process, known as N-myristoylation, is crucial for the proper functioning of various proteins involved in signal transduction, apoptosis, and cellular trafficking .
NMT1 is a protein-coding gene that plays a pivotal role in the post-translational modification of proteins. The enzyme operates by transferring myristate from myristoyl-CoA to the N-terminal glycine of target proteins. This modification is irreversible and is essential for the full expression of the biological activities of several N-myristoylated proteins .
The catalytic domain of NMT1 contains an N-terminal region that acts as an inhibitory module. This region regulates the enzyme’s activity by modulating its catalytic efficiency. Removal of this N-terminal peptide has been shown to increase the enzyme’s activity, suggesting that it serves as a regulatory control element .
NMT1 is involved in various cellular processes, including signal transduction and apoptosis. It is essential for the proper functioning of several proteins, including the alpha subunit of the signal-transducing guanine nucleotide-binding protein (G protein). The enzyme’s activity is crucial for the biological activities of these proteins, making it a central switch in cellular signaling pathways .
NMT1 has attracted significant interest as a potential therapeutic target for cancer and infectious diseases. Specific inhibitors of NMT1 have been developed and are being explored for their therapeutic potential. These inhibitors can block N-myristoylation in cells, thereby affecting the function of N-myristoylated proteins and potentially providing a therapeutic benefit .
Recent studies have focused on the validation and invalidation of chemical probes for human NMT1. These studies have identified several compounds that can selectively inhibit NMT1 activity in cells. For example, IMP-1088 has been shown to deliver complete and specific inhibition of N-myristoylation in a range of cell lines .
Additionally, research has demonstrated that the N-terminal region of the catalytic domain of NMT1 acts as an inhibitory module. This finding suggests that the proteolytic processing of this region could provide a molecular mechanism for the physiological up-regulation of NMT1 activity .
