N-myristoyltransferase 1

NMT1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1RXT, 3IU1, 3IU2, 3IWE, 3JTK, 4C2Y, 4C2Z

Identifiers

Aliases

NMT1, Nmt1, AW536594, NMT, N-myristoyltransferase 1

External IDs

MGI: 102579 HomoloGene: 69027 GeneCards: NMT1

Gene ontology
Molecular function	• transferase activity • transferase activity, transferring acyl groups • glycylpeptide N-tetradecanoyltransferase activity • myristoyltransferase activity
Cellular component	• cytosol • membrane • plasma membrane • cell junction • actin cytoskeleton • extrinsic component of membrane • cytoplasm • mitochondrion
Biological process	• regulation of rhodopsin mediated signaling pathway • in utero embryonic development • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway • N-terminal peptidyl-glycine N-myristoylation • N-terminal protein myristoylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


4836


18107

Ensembl


ENSG00000136448


ENSMUSG00000020936

UniProt


P30419


O70310

RefSeq (mRNA)


NM_021079


NM_008707

RefSeq (protein)


NP_066565.1


NP_032733.1

Location (UCSC)

Chr 17: 45.05 – 45.11 Mb

Chr 11: 103.03 – 103.07 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Glycylpeptide N-tetradecanoyltransferase 1 also known as myristoyl-CoA:protein N-myristoyltransferase 1 (NMT-1) is an enzyme that in humans is encoded by the NMT1 gene.^[3]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Duronio RJ, Reed SI, Gordon JI (May 1992). "Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae". Proc Natl Acad Sci U S A. 89 (9): 4129–33. doi:10.1073/pnas.89.9.4129. PMC 525646. PMID 1570339.
↑ "Entrez Gene: NMT1 N-myristoyltransferase 1".

Rajala RV, Datla RS, Moyana TN, et al. (2000). "N-myristoyltransferase.". Mol. Cell. Biochem. 204 (1–2): 135–55. doi:10.1023/A:1007012622030. PMID 10718634.
Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
Wice BM, Gordon JI (1992). "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". J. Cell Biol. 116 (2): 405–22. doi:10.1083/jcb.116.2.405. PMC 2289284. PMID 1530946.
Mumby SM, Heukeroth RO, Gordon JI, Gilman AG (1990). "G-protein alpha-subunit expression, myristoylation, and membrane association in COS cells". Proc. Natl. Acad. Sci. U.S.A. 87 (2): 728–32. doi:10.1073/pnas.87.2.728. PMC 53339. PMID 2153964.
Pal R, Reitz MS, Tschachler E, et al. (1990). "Myristoylation of gag proteins of HIV-1 plays an important role in virus assembly". AIDS Res. Hum. Retroviruses. 6 (6): 721–30. doi:10.1089/aid.1990.6.721. PMID 2194551.
Bryant M, Ratner L (1990). "Myristoylation-dependent replication and assembly of human immunodeficiency virus 1". Proc. Natl. Acad. Sci. U.S.A. 87 (2): 523–7. doi:10.1073/pnas.87.2.523. PMC 53297. PMID 2405382.
Tashiro A, Shoji S, Kubota Y (1990). "Antimyristoylation of the gag proteins in the human immunodeficiency virus-infected cells with N-myristoyl glycinal diethylacetal resulted in inhibition of virus production". Biochem. Biophys. Res. Commun. 165 (3): 1145–54. doi:10.1016/0006-291X(89)92722-8. PMID 2692561.
Goddard C, Aquino A, Glazer RI, Felsted RL (1989). "Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein". Eur. J. Biochem. 182 (2): 323–6. doi:10.1111/j.1432-1033.1989.tb14833.x. PMID 2737204.
Göttlinger HG, Sodroski JG, Haseltine WA (1989). "Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (15): 5781–5. doi:10.1073/pnas.86.15.5781. PMC 297714. PMID 2788277.
Schultz AM, Henderson LE, Oroszlan S, et al. (1985). "Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein". Science. 227 (4685): 427–9. doi:10.1126/science.3917576. PMID 3917576.
Liu J, Sessa WC (1994). "Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase". J. Biol. Chem. 269 (16): 11691–4. PMID 7512951.
Lee PP, Linial ML (1994). "Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal". J. Virol. 68 (10): 6644–54. PMC 237085. PMID 7521919.
Sigal CT, Zhou W, Buser CA, et al. (1995). "Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids". Proc. Natl. Acad. Sci. U.S.A. 91 (25): 12253–7. doi:10.1073/pnas.91.25.12253. PMC 45415. PMID 7527558.
Zhou W, Parent LJ, Wills JW, Resh MD (1994). "Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids". J. Virol. 68 (4): 2556–69. PMC 236733. PMID 8139035.
Kobayashi M, Takamatsu K, Saitoh S, Noguchi T (1993). "Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties". J. Biol. Chem. 268 (25): 18898–904. PMID 8360179.
Morikawa Y, Hinata S, Tomoda H, et al. (1996). "Complete inhibition of human immunodeficiency virus Gag myristoylation is necessary for inhibition of particle budding". J. Biol. Chem. 271 (5): 2868–73. doi:10.1074/jbc.271.5.2868. PMID 8576268.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Zhou W, Resh MD (1997). "Differential membrane binding of the human immunodeficiency virus type 1 matrix protein". J. Virol. 70 (12): 8540–8. PMC 190946. PMID 8970978.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.

Transferases: acyltransferases (EC 2.3)

2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5

2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII

2.3.3: converted into alkyl on transfer	Citrate synthase ATP citrate lyase HMG-CoA synthase Malate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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N-myristoyltransferase 1

References

Further reading

See also