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Gene Review

NMT1  -  N-myristoyltransferase 1

Homo sapiens

Synonyms: Glycylpeptide N-tetradecanoyltransferase 1, Myristoyl-CoA:protein N-myristoyltransferase 1, NMT, NMT 1, Peptide N-myristoyltransferase 1, ...
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Disease relevance of NMT1


Psychiatry related information on NMT1

  • A rodent model of diencephalic amnesia, pyrithiamine-induced thiamine deficiency (PTD), was used to investigate the dynamic role of hippocampal and striatal acetylcholine (ACh) efflux across acquisition of a nonmatching-to-position (NMTP) T-maze task [5].

High impact information on NMT1


Chemical compound and disease context of NMT1


Biological context of NMT1

  • Overall, the data indicate that NMT1 and NMT2 have only partially overlapping functions and that NMT1 is critical for tumor cell proliferation [13].
  • The mouse and human versions of each NMT are highly homologous, displaying greater than 95% amino acid sequence identity [14].
  • Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis [13].
  • Using RNA interference, this study functionally characterizes the two NMT isozymes in human cells [13].
  • In contrast, immunoblotting of cells transfected with a plasmid containing the smaller insert identified a approximately 50-kDa FLAG-NMT predominantly in the cytosolic fraction [3].

Anatomical context of NMT1

  • Western analysis revealed that while hNMT-2 appeared as a single 65-kDa protein in transfected COS-7 cells, hNMT-1 was processed to provide four distinct protein isoforms ranging from 49 to 68 kDa in size [14].
  • Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction [3].
  • An analysis of mixtures of CEM ribosomes and serial dilutions of purified recombinant FLAG-NMTs demonstrated that the approximately 60-kDa FLAG-NMT binds ribosomes with higher affinity than the approximately 50-kDa FLAG-NMT [3].
  • Immunoprecipitation of NMT from human cell lines and immunoblotting of a range of rat tissues has identified proteins with molecular masses corresponding to those derived from these cDNAs, and provided evidence that their relative abundance differs among tissues [15].
  • In this review article, I summarize that NMT may have a potential role in cardiac muscle in the experimentally induced ischemia-reperfusion rat model and also in the streptozotoein-induced diabetic rat [9].

Associations of NMT1 with chemical compounds

  • N-myristoyltransferases (NMT) add myristate to the NH(2) termini of certain proteins, thereby regulating their localization and/or biological function [13].
  • The AtNMT was similar to the mammalian NMTs with respect to a relative specificity for myristoyl CoA among the acyl CoA donors and also inhibition by the bovine brain NMT inhibitor NIP(71) [16].
  • The data also indicate that although the unique NH2-terminal residues encoded by this larger open reading frame are not required for in vitro catalytic activity, they do provide signal(s) involved in targeting hNMT to the ribosomal subcellular fraction where cotranslational N-myristoylation occurs [3].
  • Sucrose density gradient centrifugation of the ribosomal fraction resulted in the hNMT activity sedimenting exactly coincident with the 260 nm absorption profile and exhibiting A260/A280 absorption ratios >1.8, indicating an association of NMT with putative ribosomal particle(s)/subunit(s) [3].
  • Such interactions appear to enhance the activity of hNMT towards its serine-containing substrates [17].

Physical interactions of NMT1

  • Furthermore, protein-protein interaction of NMTs revealed that m-calpain interacts with NMT1 while caspase-3 interacts with NMT2 [1].

Other interactions of NMT1


Analytical, diagnostic and therapeutic context of NMT1


  1. N-myristoyltransferase 2 expression in human colon cancer: cross-talk between the calpain and caspase system. Selvakumar, P., Smith-Windsor, E., Bonham, K., Sharma, R.K. FEBS Lett. (2006) [Pubmed]
  2. Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review). Selvakumar, P., Sharma, R.K. Int. J. Mol. Med. (2007) [Pubmed]
  3. Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction. Glover, C.J., Hartman, K.D., Felsted, R.L. J. Biol. Chem. (1997) [Pubmed]
  4. Novel strategy for anti-HIV-1 action: selective cytotoxic effect of N-myristoyltransferase inhibitor on HIV-1-infected cells. Takamune, N., Hamada, H., Misumi, S., Shoji, S. FEBS Lett. (2002) [Pubmed]
  5. Blunted hippocampal, but not striatal, acetylcholine efflux parallels learning impairment in diencephalic-lesioned rats. Roland, J.J., Savage, L.M. Neurobiology of learning and memory (2007) [Pubmed]
  6. Nonadrenal epinephrine-forming enzymes in humans. Characteristics, distribution, regulation, and relationship to epinephrine levels. Kennedy, B., Bigby, T.D., Ziegler, M.G. J. Clin. Invest. (1995) [Pubmed]
  7. A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. Wice, B.M., Gordon, J.I. J. Cell Biol. (1992) [Pubmed]
  8. Increased excretion of dimethyltryptamine and certain features of psychosis: a possible association. Murray, R.M., Oon, M.C., Rodnight, R., Birley, J.L., Smith, A. Arch. Gen. Psychiatry (1979) [Pubmed]
  9. Potential role of N-myristoyltransferase in pathogenic conditions. Sharma, R.K. Can. J. Physiol. Pharmacol. (2004) [Pubmed]
  10. Nonmyeloablative transplantation with or without alemtuzumab: comparison between 2 prospective studies in patients with lymphoproliferative disorders. Pérez-Simón, J.A., Kottaridis, P.D., Martino, R., Craddock, C., Caballero, D., Chopra, R., García-Conde, J., Milligan, D.W., Schey, S., Urbano-Ispizua, A., Parker, A., Leon, A., Yong, K., Sureda, A., Hunter, A., Sierra, J., Goldstone, A.H., Linch, D.C., San Miguel, J.F., Mackinnon, S. Blood (2002) [Pubmed]
  11. Substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Analysis of fatty acid analogs containing carbonyl groups, nitrogen heteroatoms, and nitrogen heterocycles in an in vitro enzyme assay and subsequent identification of inhibitors of human immunodeficiency virus I replication. Devadas, B., Lu, T., Katoh, A., Kishore, N.S., Wade, A.C., Mehta, P.P., Rudnick, D.A., Bryant, M.L., Adams, S.P., Li, Q. J. Biol. Chem. (1992) [Pubmed]
  12. In vitro antiviral activities of myristic acid analogs against human immunodeficiency and hepatitis B viruses. Parang, K., Wiebe, L.I., Knaus, E.E., Huang, J.S., Tyrrell, D.L., Csizmadia, F. Antiviral Res. (1997) [Pubmed]
  13. Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis. Ducker, C.E., Upson, J.J., French, K.J., Smith, C.D. Mol. Cancer Res. (2005) [Pubmed]
  14. A second mammalian N-myristoyltransferase. Giang, D.K., Cravatt, B.F. J. Biol. Chem. (1998) [Pubmed]
  15. Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme. McIlhinney, R.A., Young, K., Egerton, M., Camble, R., White, A., Soloviev, M. Biochem. J. (1998) [Pubmed]
  16. Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana. Qi, Q., Rajala, R.V., Anderson, W., Jiang, C., Rozwadowski, K., Selvaraj, G., Sharma, R., Datla, R. J. Biol. Chem. (2000) [Pubmed]
  17. Enhanced activity of human N-myristoyltransferase by dimethyl sulfoxide and related solvents in the presence of serine/threonine-containing peptide substrates. Pasha, M.K., Dimmock, J.R., Hollenberg, M.D., Sharma, R.K. Biochem. Pharmacol. (2002) [Pubmed]
  18. Expression of N-myristoyltransferase inhibitor protein and its relationship to c-Src levels in human colon cancer cell lines. Rajala, R.V., Dehm, S., Bi, X., Bonham, K., Sharma, R.K. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  19. Expression of methionine aminopeptidase 2, N-myristoyltransferase, and N-myristoyltransferase inhibitor protein 71 in HT29. Selvakumar, P., Lakshmikuttyamma, A., Lawman, Z., Bonham, K., Dimmock, J.R., Sharma, R.K. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  20. Monitoring the expression profiles of doxorubicin-resistant K562 human leukemia cells by serial analysis of gene expression. Ichikawa, Y., Hirokawa, M., Aiba, N., Fujishima, N., Komatsuda, A., Saitoh, H., Kume, M., Miura, I., Sawada, K. Int. J. Hematol. (2004) [Pubmed]
  21. Overexpression of human N-myristoyltransferase utilizing a T7 polymerase gene expression system. Raju, R.V., Datla, R.S., Sharma, R.K. Protein Expr. Purif. (1996) [Pubmed]
  22. Phosphorylation of human N-myristoyltransferase by N-myristoylated SRC family tyrosine kinase members. Rajala, R.V., Datla, R.S., Carlsen, S.A., Anderson, D.H., Qi, Z., Wang, J.H., Sharma, R.K. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  23. N-myristoyltransferase. Rajala, R.V., Datla, R.S., Moyana, T.N., Kakkar, R., Carlsen, S.A., Sharma, R.K. Mol. Cell. Biochem. (2000) [Pubmed]
  24. N-Myristoyltransferase overexpression in human colorectal adenocarcinomas. Raju, R.V., Moyana, T.N., Sharma, R.K. Exp. Cell Res. (1997) [Pubmed]
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