EC Number   |
General Information |
Reference |
|---|
   2.3.1.97 | evolution |
N-myristoyltransferase is an ubiquitously distributed enzyme and belongs to the GCN5 acetyltransferase superfamily. NMT exists as a single copy gene in lower eukaryotes, whereas in higher eukaryotes, two genes encoding for the two isoforms of NMT have been identified. The NMT1 isoform is homologous to the NMT from lower eukaryotes |
719244 |
| 2.3.1.97 | malfunction |
enzyme knockout leads to defective myelopoesis |
704940 |
| 2.3.1.97 | malfunction |
expression of isozyme NMT1 is reduced in lung inflammation and induced by Mannheimer hemolytica, probably due to increased enolase expression |
706890 |
| 2.3.1.97 | malfunction |
NMT plays a role in epilepsy |
706573 |
| 2.3.1.97 | malfunction |
NMT2 is not able to rescue N-myristoylation of proteins for the proper development of the embryos in NMT1-/- mice knockouts, the embryos die during early embryogenesis. Bone marrow cells taken from wild-type and heterozygous Nmt1-deficient mice and cultured in the presence of mouse macrophage colony-stimulating factor for differentiation into monocytes/macrophages develop in a different manner, overview |
719244 |
| 2.3.1.97 | metabolism |
both N-myristoyltransferases NMT1 and NMT2 are cleaved during apoptosis. The caspase-3- or -8-mediated cleavage of NMT1 at Asp72 precedes the cleavage of NMT2 by caspase-3 mainly at Asp25. The cleavage of NMTs does not significantly affect their activity in apoptotic cells until the 8 h time point. The cleavage of the predominantly membrane bound NMT1 removes a polybasic domain stretch and leads to a cytosolic relocalization, whereas predominantly cytosolic NMT2 relocalizes to membranes when cleaved after the removal of a negatively charged domain |
736079 |
| 2.3.1.97 | more |
human NMT-1 specifically myristoylates Nef and the two proteins are able to remain associated through immunoprecipitation and purification steps, Nef:NMT complex structure analysis, overview |
718896 |
| 2.3.1.97 | physiological function |
acyl-CoA binding protein, acyl-CoA binding domain (ACBD)6, stimulates the myristoyltransferase reaction of isoform NMT2. The stimulatory effect requires interaction between ACBD6 and NMT2, and is enhanced by binding of ACBD6 to its ligand, C18:2 -CoA. The presence of ACBD6 prevents competition of the myristoyltransferase reaction by C16 -CoA. Mutants of ACBD6 that are either deficient in ligand binding to the N-terminal ACBD or unable to interact with NMT2 do not stimulate activity of NMT2, nor can they protect the enzyme from utilizing the competitor C16 -CoA |
757371 |
| 2.3.1.97 | physiological function |
expression in Escherichia coli mutant having lipid A containing only 3-hydroxymyristic acids, leads to lipid A with two additional myristic acids (C14:0). When the gene is introduced into a mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0. C12:0 in lipid A can be replaced by C14:0 without changing the immunostimulating activity |
-, 757615 |
| 2.3.1.97 | physiological function |
expression of NMT gene is essential for survival of Trypanosoma cruzi epimastigotes |
735635 |
