In enzymology, a glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) is an enzyme that catalyzes the chemical reaction
tetradecanoyl-CoA + glycylpeptide ⇌ {\displaystyle \rightleftharpoons } CoA + N-tetradecanoylglycylpeptide Thus, the two substrates of this enzyme are tetradecanoyl-CoA and glycylpeptide, whereas its two products are CoA and N-tetradecanoylglycylpeptide. It participates in the N-Myristoylation of proteins, and in vertebrates there are two isoenzymes NMT1 and NMT2. Besides tetradecanoyl-CoA, this enzyme is also capable of using modified versions of this substrate. In human retina, an even wider range of fatty acids, including 14:1 n–9, 14:2n–6, and 12:0, are accepted by the enzyme and grafted onto guanylate cyclase activators. This is mainly a result of a special set of fatty-acid-CoA substrates available in the retina.
Nomenclature This enzyme belongs to the family of transferases, specifically those N-acyltransferases transferring groups other than aminoacyl groups (cd04301). The systematic name of this enzyme class is tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase. Other names in common use include peptide N-myristoyltransferase (NMT), myristoyl-CoA-protein N-myristoyltransferase, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoylating enzymes, and protein N-myristoyltransferase.
Structural studies As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1IIC, PDB: 1IID, PDB: 1IYK, PDB: 1IYL, PDB: 1RXT, PDB: 2NMT, PDB: 2P6E, PDB: 2P6F, and PDB: 2P6G. The enzyme folds into two domains, each with a double EF-hand arrangement.
References
Guertin D, Grise-Miron L, Riendeau D (1986). "Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue". Biochem. Cell Biol. 64 (12): 1249–55. Bibcode:1986BCB....64.1249G. doi:10.1139/o86-164. PMID 3566958.


