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NMT1
Available structures
PDB	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	OMIM: 160993 MGI: 102579 HomoloGene: 69027 GeneCards: NMT1
Gene location (Human)
Chr.	Chromosome 17 (human)
End	45,109,016 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	102,959,738 bp
RNA expression pattern
	Top expressed in
	Top expressed in
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
	Sources:Amigo / QuickGO
Orthologs
	4836
	18107
	ENSG00000136448
	ENSMUSG00000020936
	P30419
	O70310
	NM_021079
	NM_008707
	NP_066565
	NP_032733
	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.^[5]^[6] It belongs to the protein N-terminal methyltransferase and glycylpeptide N-tetradecanoyltransferase family of enzymes.

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000136448 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020936 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1992PNAS...89.4129D. doi:10.1073/pnas.89.9.4129. PMC 525646. PMID 1570339.
^ "Entrez Gene: NMT1 N-myristoyltransferase 1".

Further reading[edit]

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. S2CID 264010084.
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. Bibcode:1990PNAS...87..728M. 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. Bibcode:1990PNAS...87..523B. 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. Bibcode:1989PNAS...86.5781G. 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. Bibcode:1985Sci...227..427S. 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. doi:10.1016/S0021-9258(17)32626-1. 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. doi:10.1128/JVI.68.10.6644-6654.1994. 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. doi:10.1128/JVI.68.4.2556-2569.1994. 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. doi:10.1016/S0021-9258(17)46711-1. 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. doi:10.1128/JVI.70.12.8540-8548.1996. 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.

External links[edit]

Overview of all the structural information available in the PDB for UniProt: P30419 (Glycylpeptide N-tetradecanoyltransferase 1) at the PDBe-KB.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000136448 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020936 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1570339-5] 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. Bibcode:1992PNAS...89.4129D. doi:10.1073/pnas.89.9.4129. PMC 525646. PMID 1570339.

[entrez-6] "Entrez Gene: NMT1 N-myristoyltransferase 1".

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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 Decylcitrate synthase Citrate (Re)-synthase Decylhomocitrate synthase 2-methylcitrate synthase 2-ethylmalate synthase 3-ethylmalate synthase ATP citrate lyase Malate synthase HMG-CoA synthase HMGCS2 2-hydroxyglutarate synthase 3-propylmalate synthase 2-isopropylmalate synthase Homocitrate synthase Sulfoacetaldehyde acetyltransferase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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