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Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase and Organism(s) Plasmodium falciparum and UniProt Accession Q8ILW6

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IUBMB Comments
The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
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Plasmodium falciparum
UNIPROT: Q8ILW6
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The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-myristoyltransferase, nmt-1, myristoyl-coa:protein n-myristoyltransferase, n-myristoyl transferase, nmt1p, n-myristoyltransferase 1, myristoyltransferase, canmt, myristoyl-coa protein n-myristoyltransferase, tbnmt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-myristoyltransferase
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myristoyl-CoA-protein N-myristoyltransferase
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myristoyl-CoA:protein N-myristoyltransferase
myristoyl-coenzyme A:protein N-myristoyl transferase
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myristoylating enzymes
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myristoyltransferase, protein N-
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N-myristoyltransferase
peptide N-myristoyltransferase
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protein N-myristoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
show the reaction diagram
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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amide bond formation
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SYSTEMATIC NAME
IUBMB Comments
tetradecanoyl-CoA:N-terminal-glycine-[protein] N-tetradecanoyltransferase
The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
CAS REGISTRY NUMBER
COMMENTARY hide
110071-61-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + peptide CAP5.5
CoA + N-myristoyl-peptide CAP5.5
show the reaction diagram
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein
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?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
show the reaction diagram
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i.e. myristoyl-CoA
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?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
show the reaction diagram
i.e. myristoyl-CoA, the enzyme attaches the fatty acid to a glycine at the N-terminus of a number of eukaryotic cellular and viral proteins
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?
additional information
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-N-(2-cyclohexylethyl)-2-[[N-([3-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetyl)-L-seryl]amino]heptanamide
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(3R)-3-amino-4-(4-chlorophenyl)-1-[(3R,4S)-3-(hydroxymethyl)-4-(4-methoxyphenyl)pyrrolidin-1-yl]butan-1-one
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(3R)-3-amino-4-(4-chlorophenyl)-1-[(3S,4R)-3-(4-chlorophenyl)-4-(hydroxymethyl)pyrrolidin-1-yl]butan-1-one
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1-(5-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-(2,4-difluorobenzyl)azetidine-3-carboxamide
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1-(5-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-[(5-methylpyrazin-2-yl)methyl]azetidine-3-carboxamide
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2-(4-fluorophenyl)-N-[3-(piperidin-4-yl)-1H-indol-5-yl]acetamide
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2-([[trans-4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
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5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
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N,N-dimethyl-1-[5-(2-methylphenyl)-1H-indazol-3-yl]methanamine
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N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
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N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
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[4-[3-(benzylamino)propoxy]-3-methyl-1-benzofuran-2-yl](1-methyl-1H-imidazol-2-yl)methanone
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(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
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(4S,5aS,12aS)-2-carbamoyl-4-(dimethylamino)-3,10,12,12a-tetrahydroxy-6-methylidene-1,11-dioxo-1,4,4a,5,5a,6,11,12a-octahydrotetracen-5-yl acetate
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1-hydroxy-2-[(1-methylethyl)amino]ethyl 2,6-dihydroxybenzoate
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2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
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2-([[(1R,3S)-3-[[(5-chloro-7-methylnaphthalen-2-yl)methyl]amino]cyclohexyl]acetyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-[([(1R,3S)-3-[(1-benzofuran-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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2-[([(1R,3S)-3-[(1H-indol-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
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3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
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4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5,6-trihydroxycyclohexa-2,4-diene-1-carboxamide
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4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5-dihydroxybenzamide
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4-[(2-[5-[(1,3,5-trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl]-1-benzothiophen-3-yl)oxy]piperidine
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selective and high affinity inhibitor, pKi value 8.10
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
cis-N-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
cis-N-1,3-benzothiazol-2-yl-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
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ethyl 4-(ethylsulfanyl)-6-([6-[(piperidin-4-yl)amino]pyridin-3-yl]methoxy)quinoline-3-carboxylate
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ethyl 4-(ethylsulfanyl)-6-[(6-[[(3R)-pyrrolidin-3-yl]amino]pyridin-3-yl)methoxy]quinoline-3-carboxylate
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ethyl 4-(ethylsulfanyl)-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
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ethyl 4-[(2-cyanoethyl)sulfanyl]-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
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ethyl 6-(benzyloxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
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ethyl 6-([6-[(2-aminoethyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
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ethyl 6-([6-[(3-aminopropyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
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N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
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peptidomimetic inhibitor
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
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N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
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S-(2-oxo)pentadecyl-CoA
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additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
ethyl 4-(ethylsulfanyl)-6-([6-[(piperidin-4-yl)amino]pyridin-3-yl]methoxy)quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
0.00096
ethyl 4-(ethylsulfanyl)-6-[(6-[[(3R)-pyrrolidin-3-yl]amino]pyridin-3-yl)methoxy]quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
0.00024
ethyl 4-(ethylsulfanyl)-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
0.00331
ethyl 4-[(2-cyanoethyl)sulfanyl]-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
0.00067
ethyl 6-(benzyloxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
0.00125
ethyl 6-([6-[(2-aminoethyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
0.00015
ethyl 6-([6-[(3-aminopropyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
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pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0243
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Plasmodium falciparum
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pH not specified in the publication, temperature not specified in the publication
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
sequence comparisons
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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the enzyme is a drug target
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bowyer, P.; Tate, E.; Leatherbarrow, R.; Holder, A.; Smith, D.; Brown, K.
N-myristoyltransferase: A prospective drug target for protozoan parasites
ChemMedChem
3
402-408
2008
Histoplasma capsulatum, Saccharomyces cerevisiae, Candida albicans, Cryptococcus neoformans, Leishmania major, Plasmodium falciparum, Trypanosoma brucei
Manually annotated by BRENDA team
Sheng, C.; Ji, H.; Miao, Z.; Che, X.; Yao, J.; Wang, W.; Dong, G.; Guo, W.; Lue, J.; Zhang, W.
Homology modeling and molecular dynamics simulation of N-myristoyltransferase from protozoan parasites: active site characterization and insights into rational inhibitor design
J. Comput. Aided Mol. Des.
23
375-389
2009
Trypanosoma brucei, Leishmania major (Q9GPZ4), Leishmania major, Plasmodium falciparum (Q9U419), Plasmodium falciparum
Manually annotated by BRENDA team
Bell, A.S.; Mills, J.E.; Williams, G.P.; Brannigan, J.A.; Wilkinson, A.J.; Parkinson, T.; Leatherbarrow, R.J.; Tate, E.W.; Holder, A.A.; Smith, D.F.
Selective inhibitors of protozoan protein N-myristoyltransferases as starting points for tropical disease medicinal chemistry programs
PLoS Negl. Trop. Dis.
6
e1625
2012
Trypanosoma brucei (D0A003), Trypanosoma brucei, Leishmania donovani (D0AB09), Leishmania donovani, Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens, Plasmodium falciparum (Q8ILW6), Plasmodium falciparum
Manually annotated by BRENDA team
Olaleye, T.O.; Brannigan, J.A.; Roberts, S.M.; Leatherbarrow, R.J.; Wilkinson, A.J.; Tate, E.W.
Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites
Org. Biomol. Chem.
12
8132-8137
2014
Plasmodium falciparum, Plasmodium vivax (A5K1A2), Leishmania donovani (D0AB09), Homo sapiens (P30419), Homo sapiens, Plasmodium vivax Salvador I (A5K1A2)
Manually annotated by BRENDA team
Garcia, M.; de Oliveira, A.; Bueno, R.; Nogueira, V.; de Souza, G.; Guido, R.
QSAR studies on benzothiophene derivatives as Plasmodium falciparum N-myristoyltransferase inhibitors Molecular insights into affinity and selectivity
Drug Dev. Res.
2020
1-21
2020
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Goncalves, V.; Brannigan, J.; Laporte, A.; Bell, A.; Roberts, S.; Wilkinson, A.; Leatherbarrow, R.; Tate, E.
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
MedChemComm
8
191-197
2017
Plasmodium falciparum, Plasmodium vivax (A5K1A2), Plasmodium vivax, Homo sapiens (O60551), Homo sapiens (P30419), Plasmodium vivax Salvador I (A5K1A2)
Manually annotated by BRENDA team