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Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase and Organism(s) Homo sapiens and UniProt Accession O60551

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EC Tree
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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Homo sapiens
UNIPROT: O60551
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
glycylpeptide N-tetradecanoyltransferase 2
-
myristoyl-CoA:protein N-myristoyltransferase 2
-
myristoyltransferase
-
N-myristoyltransferase
-
peptide N-myristoyltransferase 2
-
type II N-myristoyltransferase
-
myristoyl-CoA-protein N-myristoyltransferase
-
-
-
-
myristoyl-CoA:protein N-myristoyltransferase
-
-
myristoyl-CoA:protein N-myristoyltransferase 1
-
myristoyl-coenzyme A:protein N-myristoyl transferase
-
-
-
-
myristoyl-coenzyme A:protein N-myristoyltransferase
-
-
myristoylating enzymes
-
-
-
-
myristoyltransferase
myristoyltransferase type 1
-
myristoyltransferase, protein N-
-
-
-
-
N-myristoyltransferase
N-myristoyltransferase 1
-
-
N-myristoyltransferase 2
-
-
NMT-2
-
-
peptide N-myristoyltransferase
-
-
-
-
peptide N-myristoyltransferase 1
-
protein N-myristoyltransferase
-
-
-
-
type I N-myristoyltransferase
-
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
Acyl group transfer
-
-
-
-
amide bond formation
-
-
-
-
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
-
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 + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
show the reaction diagram
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
show the reaction diagram
cAMP-dependent protein kinase-derived peptide
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
myristoyl-CoA + HIV1 Gag protein N-terminal peptide
N-myristoyl-HIV1 Gag protein N-terminal peptide + CoA
show the reaction diagram
-
-
-
?
myristoyl-CoA + HIV1 Nef protein N-terminal peptide
N-myristoyl-HIV1 Nef protein N-terminal peptide + CoA
show the reaction diagram
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
show the reaction diagram
decapeptide, best substrate
-
-
?
myristoyl-CoA + tumor necrosis factor-derived peptide
N-myristoylated tumor necrosis factor-derived peptide + CoA
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
show the reaction diagram
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
show the reaction diagram
lauroyl-CoA + brain acid soluble protein 1
N-lauroyl-brain acid soluble protein 1 + CoA
show the reaction diagram
-
-
N-laurylation of recombinant proteins in Escherichia coli may occur in minimal media
-
?
lauroyl-CoA + c-Src
N-lauroyl-c-Src + CoA
show the reaction diagram
-
N-terminal region of c-Src, residues 1-185
N-laurylation of recombinant proteins in Escherichia coli may occur in minimal media
-
?
myristoyl-CoA + brain acid soluble protein 1
N-myristoyl-brain acid soluble protein 1 + CoA
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + c-Src
N-myristoyl-c-Src + CoA
show the reaction diagram
-
N-terminal region of c-Src, residues 1-185
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
show the reaction diagram
myristoyl-CoA + Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg
N-myristoyl-Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg-derived peptide + CoA
show the reaction diagram
-
i.e. myristolated alanine-rich C-kinase substrate MARCKS
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
show the reaction diagram
cAMP-dependent protein kinase-derived peptide
-
-
?
myristoyl-CoA + Gly-Cys-Ser-Val-Ser-Lys-Lys-Lys
CoA + N-myristoyl-Gly-Cys-Ser-Val-Ser-Lys-Lys-Lys
show the reaction diagram
-
-
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg + CoA
show the reaction diagram
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
myristoyl-CoA + GNAASARR
?
show the reaction diagram
-
-
-
?
myristoyl-CoA + HBV preS1
? + CoA
show the reaction diagram
-
N-myristoylation of HBV preS1 is essential for viral infectivity. HBV preS1 is a fusion protein of hepatitis B virus preS1 with the native-type N-terminus and a His6-Tag fused to C-terminus
-
-
?
myristoyl-CoA + HBV preS1-HT
? + CoA
show the reaction diagram
-
fusion protein of hepatitis B virus preS1 with the native-type N-terminus and a His6-Tag fused to C-terminus
-
-
?
myristoyl-CoA + HIV-1 Nef protein
?
show the reaction diagram
-
myristoylation results in conformational changes in HIV-1 Nef
-
-
?
myristoyl-CoA + HIV-1 negative regulatory factor
N-myristoyl-HIV-1 negative regulatory factor + CoA
show the reaction diagram
-
-
-
?
myristoyl-CoA + HIV1 Gag protein N-terminal peptide
N-myristoyl-HIV1 Gag protein N-terminal peptide + CoA
show the reaction diagram
-
-
-
?
myristoyl-CoA + HIV1 Nef protein N-terminal peptide
N-myristoyl-HIV1 Nef protein N-terminal peptide + CoA
show the reaction diagram
-
-
-
?
myristoyl-CoA + M2 gene segment of reovirus type 3-derived peptide
N-myristoylated M2 gene segment of reovirus type 3-derived peptide + CoA
show the reaction diagram
-
i.e. Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys
-
-
?
myristoyl-CoA + Nef
? + CoA
show the reaction diagram
-
Nef forms a stable complex specifically with N-myristoyltransferase isoform 1. The association requires an N–terminal region of Nef containing an intact myristoylation signal and represents a transient intermediate of the myristoylation reaction
-
-
?
myristoyl-CoA + Nef protein
CoA + N-myristoyl-Nef protein
show the reaction diagram
-
HIV-1 accessory protein Nef, usage of C-terminally 6xHis-tagged Nef SF2
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
show the reaction diagram
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
-
-
?
myristoyl-CoA + peptide Hs pp60src(2-9)
CoA + N-myristoyl-peptideHs pp60src(2-9)
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + tumor necrosis factor-derived peptide
N-myristoylated tumor necrosis factor-derived peptide + CoA
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
show the reaction diagram
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
show the reaction diagram
tetradecanoyl-CoA + glycyl-pp60c-Src
CoA + N-tetradecanoyl-glycyl-pp60c-Src
show the reaction diagram
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
N-myristoylation is a process of covalent irreversible protein modification that promotes association of proteins with membranes
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
show the reaction diagram
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
myristoyl-CoA + HBV preS1
? + CoA
show the reaction diagram
-
N-myristoylation of HBV preS1 is essential for viral infectivity. HBV preS1 is a fusion protein of hepatitis B virus preS1 with the native-type N-terminus and a His6-Tag fused to C-terminus
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + glycyl-pp60c-Src
CoA + N-tetradecanoyl-glycyl-pp60c-Src
show the reaction diagram
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R)-3-amino-4-(4-chlorophenyl)-1-[(3R,4S)-3-(hydroxymethyl)-4-(4-methoxyphenyl)pyrrolidin-1-yl]butan-1-one
-
(3R)-3-amino-4-(4-chlorophenyl)-1-[(3S,4R)-3-(4-chlorophenyl)-4-(hydroxymethyl)pyrrolidin-1-yl]butan-1-one
-
1-(5-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-(2,4-difluorobenzyl)azetidine-3-carboxamide
-
1-(5-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-[(5-methylpyrazin-2-yl)methyl]azetidine-3-carboxamide
-
1-(5-[3,4-difluoro-2-[2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethoxy]phenyl]-1-methyl-1H-indazol-3-yl)-N,N-dimethylmethanamine
-
2-(4-fluorophenyl)-N-[3-(piperidin-4-yl)-1H-indol-5-yl]acetamide
-
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
-
5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
-
ethyl 4-(ethylsulfanyl)-6-([6-[(piperidin-4-yl)amino]pyridin-3-yl]methoxy)quinoline-3-carboxylate
-
ethyl 4-(ethylsulfanyl)-6-[(6-[[(3R)-pyrrolidin-3-yl]amino]pyridin-3-yl)methoxy]quinoline-3-carboxylate
-
ethyl 4-(ethylsulfanyl)-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
-
ethyl 4-[(2-cyanoethyl)sulfanyl]-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
-
ethyl 6-(benzyloxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
-
ethyl 6-([6-[(2-aminoethyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
-
ethyl 6-([6-[(3-aminopropyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
-
HIV1 Nef protein N-terminal peptide
Nef peptide acts as a competitive inhibitor for the myristoylation of Gag
-
N,N-dimethyl-1-[5-(2-methylphenyl)-1H-indazol-3-yl]methanamine
-
N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
-
N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
-
(3R)-3-amino-4-(4-chlorophenyl)-1-[(3R,4S)-3-(hydroxymethyl)-4-(4-methoxyphenyl)pyrrolidin-1-yl]butan-1-one
-
(3R)-3-amino-4-(4-chlorophenyl)-1-[(3S,4R)-3-(4-chlorophenyl)-4-(hydroxymethyl)pyrrolidin-1-yl]butan-1-one
-
1,12-dodecanedicarboxylic acid
IC50 above 100 mM
1,3-dimyristoylglycerol
IC50 above 100 mM
1-(5-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-(2,4-difluorobenzyl)azetidine-3-carboxamide
-
1-(5-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-[(5-methylpyrazin-2-yl)methyl]azetidine-3-carboxamide
-
1-(5-[3,4-difluoro-2-[2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethoxy]phenyl]-1-methyl-1H-indazol-3-yl)-N,N-dimethylmethanamine
-
1-myristoyl-rac-glycerol
IC50 in the range 1-100 mM
1-Tetradecanal
IC50 in the range 1-100 mM
1-Tetradecanol
IC50 above 100 mM
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2-(4-fluorophenyl)-N-[3-(piperidin-4-yl)-1H-indol-5-yl]acetamide
-
2-dodecylglycidoyl-S-CoA
IC50 below 1 mM
2-[(2-methylpropanoyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
14% inhibition at 0.01 mM
2-[(cyclobutylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
22% inhibition at 0.01 mM
2-[(cyclohexanecarbonyl)amino]-N-[(2-naphthylmethyl)amino]ethyl-benzothiazole-6-carboxamide
49% inhibition at 0.01 mM
2-[(cyclohexylcarbonyl)amino]-N-[3-[(naphthalen-2-ylmethyl)amino]propyl]-1,3-benzothiazole-6-carboxamide
61% inhibition at 0.01 mM
2-[(cyclohexylcarbonyl)amino]-N-[4-[(naphthalen-2-ylmethyl)amino]butyl]-1,3-benzothiazole-6-carboxamide
43% inhibition at 0.01 mM
2-[(cyclohexylcarbonyl)amino]-N-[5-[(naphthalen-2-ylmethyl)amino]pentyl]-1,3-benzothiazole-6-carboxamide
46% inhibition at 0.01 mM
2-[(cyclopentylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
32% inhibition at 0.01 mM
2-[[(2,5-dimethoxyphenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
71% inhibition at 0.01 mM
2-[[(2-chloropyridin-3-yl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
16% inhibition at 0.01 mM
2-[[(3,4-dichlorophenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
22% inhibition at 0.01 mM
2-[[(4-chlorophenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
8% inhibition at 0.01 mM
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
-
3-tetradecyn-1-ol
IC50 above 100 mM
4-[(2-[5-[(1,3,5-trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl]-1-benzothiophen-3-yl)oxy]piperidine
-
selective and high affinity Plasmodium falciparum inhibitor, pKi value for human enzyme 7.22
5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
-
DDD85646
ethyl 4-(ethylsulfanyl)-6-([6-[(piperidin-4-yl)amino]pyridin-3-yl]methoxy)quinoline-3-carboxylate
-
ethyl 4-(ethylsulfanyl)-6-[(6-[[(3R)-pyrrolidin-3-yl]amino]pyridin-3-yl)methoxy]quinoline-3-carboxylate
-
ethyl 4-(ethylsulfanyl)-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
-
ethyl 4-[(2-cyanoethyl)sulfanyl]-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
-
ethyl 6-(benzyloxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
-
ethyl 6-([6-[(2-aminoethyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
-
ethyl 6-([6-[(3-aminopropyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
-
factor NIP71
-
heat shock cognate protein 70
-
involved in NMT1 regulation, overview
-
histamine
-
noncompetitive
HIV1 Nef protein N-terminal peptide
Nef peptide acts as a competitive inhibitor for the myristoylation of Gag
-
L-histidinol
-
noncompetitive, reversible by L-histidine
lauric acid
IC50 below 1 mM
myristelaidic acid
IC50 below 1 mM
myristic acid
IC50 in the range 1-100 mM
myristoleic acid
IC50 below 1 mM
N(2-S-CoA-tetradecanoyl)glycinamide
IC50 below 1 mM
N,N-dimethyl-1-[5-(2-methylphenyl)-1H-indazol-3-yl]methanamine
-
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
peptidomimetic inhibitor
N-(11-aminoundecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-(6-[[N-(naphthalen-2-ylmethyl)-b-alanyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
32% inhibition at 0.01 mM
N-(6-[[N-(naphthalen-2-ylmethyl)glycyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
8% inhibition at 0.01 mM
N-myristoyltransferase inhibitor protein 71
-
-
-
N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
-
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-(propanoylamino)-1,3-benzothiazole-6-carboxamide
4% inhibition at 0.01 mM
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-([[4-(trifluoromethyl)phenyl]carbonyl]amino)-1,3-benzothiazole-6-carboxamide
1% inhibition at 0.01 mM
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(phenylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
32% inhibition at 0.01 mM
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyrazin-2-ylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
11% inhibition at 0.01 mM
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyridin-2-ylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
37% inhibition at 0.01 mM
N-[6-([3-[(naphthalen-2-ylmethyl)amino]azetidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
14% inhibition at 0.01 mM
N-[6-([3-[(naphthalen-2-ylmethyl)amino]piperidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
27% inhibition at 0.01 mM
N-[6-([3-[(naphthalen-2-ylmethyl)amino]pyrrolidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
36% inhibition at 0.01 mM
N-[6-([4-[(naphthalen-2-ylmethyl)amino]piperidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
27% inhibition at 0.01 mM
N-[6-[(4-[[(naphthalen-2-ylmethyl)amino]methyl]piperidin-1-yl)carbonyl]-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
32% inhibition at 0.01 mM
N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
-
palmitic acid
IC50 in the range 1-100 mM
S-(2-bromotetradecanoyl)-CoA
IC50 below 1 mM
S-(2-ketopentadecyl)-CoA
IC50: 0.00006 mM
tetradecyl trimethylammonium bromide
IC50 above 100 mM
tetradecyl triphenylphosphonium bromide
IC50 above 100 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetonitrile
-
2.5fold activation at 5% v/v
dimethyl ammonium chloride
-
6.5fold increase in activity with Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg as substrate, 2.5fold increase with Gly-Asn-Ala-Ala-Ala-Ala-Lys-Lys-Arg-Arg
Dimethylsulfoxide
ethanol
-
5fold activation at 10% v/v
L-histidine
-
activation in a concentration dependent manner
SDS
-
3.2fold activation at 1.73 mM
Tris
-
activates about 2.5fold at 225 mM compared to 40 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.196 - 0.33
HIV1 Gag protein N-terminal peptide
-
0.0015 - 0.011
HIV1 Nef protein N-terminal peptide
-
0.2
cAMP-dependent protein kinase-derived peptide
-
-
-
0.0144 - 0.0257
HIV-1 negative regulatory factor
-
0.196 - 0.33
HIV1 Gag protein N-terminal peptide
-
0.0015 - 0.011
HIV1 Nef protein N-terminal peptide
-
0.195
L-histidine
-
-
0.00057 - 0.765
myristoyl-CoA
0.00276 - 0.00277
peptide Hs pp60src(2-9)
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.107 - 0.265
HIV1 Gag protein N-terminal peptide
-
0.032 - 0.052
HIV1 Nef protein N-terminal peptide
-
0.107 - 0.265
HIV1 Gag protein N-terminal peptide
-
0.032 - 0.052
HIV1 Nef protein N-terminal peptide
-
0.16 - 1.33
myristoyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.98 - 1
HIV1 Gag protein N-terminal peptide
-
4.9 - 23.6
HIV1 Nef protein N-terminal peptide
-
0.98 - 1
HIV1 Gag protein N-terminal peptide
-
4.9 - 23.6
HIV1 Nef protein N-terminal peptide
-
0.206 - 25.85
myristoyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00069
ethyl 4-(ethylsulfanyl)-6-([6-[(piperidin-4-yl)amino]pyridin-3-yl]methoxy)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00037
ethyl 4-(ethylsulfanyl)-6-[(6-[[(3R)-pyrrolidin-3-yl]amino]pyridin-3-yl)methoxy]quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.0001
ethyl 4-(ethylsulfanyl)-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00135
ethyl 4-[(2-cyanoethyl)sulfanyl]-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00423
ethyl 6-(benzyloxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00041
ethyl 6-([6-[(2-aminoethyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.0001
ethyl 6-([6-[(3-aminopropyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00008
ethyl 4-(ethylsulfanyl)-6-([6-[(piperidin-4-yl)amino]pyridin-3-yl]methoxy)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00005
ethyl 4-(ethylsulfanyl)-6-[(6-[[(3R)-pyrrolidin-3-yl]amino]pyridin-3-yl)methoxy]quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00004
ethyl 4-(ethylsulfanyl)-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00037
ethyl 4-[(2-cyanoethyl)sulfanyl]-6-[[6-(piperazin-1-yl)pyridin-3-yl]methoxy]quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00156
ethyl 6-(benzyloxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.00005
ethyl 6-([6-[(2-aminoethyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
0.000008
ethyl 6-([6-[(3-aminopropyl)amino]pyridin-3-yl]methoxy)-4-(ethylsulfanyl)quinoline-3-carboxylate
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001
1-(5-[3,4-difluoro-2-[2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethoxy]phenyl]-1-methyl-1H-indazol-3-yl)-N,N-dimethylmethanamine
Homo sapiens
IC50 value below 1 nM, pH not specified in the publication, temperature not specified in the publication
100
1,12-dodecanedicarboxylic acid
Homo sapiens
IC50 above 100 mM
100
1,3-dimyristoylglycerol
Homo sapiens
IC50 above 100 mM
0.000001
1-(5-[3,4-difluoro-2-[2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethoxy]phenyl]-1-methyl-1H-indazol-3-yl)-N,N-dimethylmethanamine
Homo sapiens
IC50 value below 1 nM, pH not specified in the publication, temperature not specified in the publication
1 - 100
1-myristoyl-rac-glycerol
Homo sapiens
IC50 in the range 1-100 mM
1 - 100
1-Tetradecanal
Homo sapiens
IC50 in the range 1-100 mM
100
1-Tetradecanol
Homo sapiens
IC50 above 100 mM
0.0000137 - 0.0000144
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
1
2-dodecylglycidoyl-S-CoA
Homo sapiens
IC50 below 1 mM
100
3-tetradecyn-1-ol
Homo sapiens
IC50 above 100 mM
1
lauric acid
Homo sapiens
IC50 below 1 mM
1
myristelaidic acid
Homo sapiens
IC50 below 1 mM
1 - 100
myristic acid
Homo sapiens
IC50 in the range 1-100 mM
1
myristoleic acid
Homo sapiens
IC50 below 1 mM
1
N(2-S-CoA-tetradecanoyl)glycinamide
Homo sapiens
IC50 below 1 mM
0.00006
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000349 - 0.000513
N-(11-aminoundecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
1 - 100
palmitic acid
Homo sapiens
IC50 in the range 1-100 mM
1
S-(2-bromotetradecanoyl)-CoA
Homo sapiens
IC50 below 1 mM
0.00006
S-(2-ketopentadecyl)-CoA
Homo sapiens
IC50: 0.00006 mM
100
tetradecyl trimethylammonium bromide
Homo sapiens
IC50 above 100 mM
100
tetradecyl triphenylphosphonium bromide
Homo sapiens
IC50 above 100 mM
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000039
recombinant enzyme from COS-7 cells
0.0000055
-
cytosol fraction, HeLa cells
0.000035
recombinant enzyme from COS-7 cells
0.248
-
purified wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9 - 8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
elevated NMT activity and higher protein expressions. Higher NMT activity in WHO grade I malignancy, compared with others of higher WHO grades
Manually annotated by BRENDA team
overexpression of NMT2 in colorectal cancer tissues
Manually annotated by BRENDA team
elevated NMT activity and higher protein expressions. Higher NMT activity in WHO grade I malignancy, compared with others of higher WHO grades
Manually annotated by BRENDA team
-
the myristoylated tyrosine kinases, pp60c-src and pp60c-yes, are observed to be several fold higher in colonic preneoplastic lesions and neoplasms compared with normal colon cells
Manually annotated by BRENDA team
-
the myristoylated tyrosine kinases, pp60c-src and pp60c-yes, are observed to be several fold higher in colonic preneoplastic lesions and neoplasms compared with normal colon cells
Manually annotated by BRENDA team
-
overexpression of NMT2. Caspase-3 interacts with NMT2
Manually annotated by BRENDA team
-
erythroleukemia cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
malfunction
-
NMT plays a role in epilepsy
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
physiological function
additional information
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NMT2_HUMAN
498
0
56980
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
1 * 65000, isoform 2, SDS-PAGE
48000
49000
-
1 * 49000, tag cleaved off by enterokinase, SDS-PAGE
60000
-
1 * 60000, recombinant h28NMT, SDS-PAGE
62000
-
1 * 62000, native from, SDS-PAGE
63000
-
x * 63000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 65000, isoform 2, SDS-PAGE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
NMT is phosphorylated by non-receptor tyrosine kinase family members of Lyn, Fyn, and Lck and dephosphorylated by the Ca2+/calmodulin-dependent protein phosphatase, calcineurin
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NMT1 structures in complex with reactive cognate lipid and peptide substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E289G
-
site-directed mutagenesis, 37.8% remaining activity
E289G/E290G
-
site-directed mutagenesis, no remaining activity
E289G/E290G/E292G
-
site-directed mutagenesis, no remaining activity
E289G/E292G
-
site-directed mutagenesis, 7% remaining activity
E290G
-
site-directed mutagenesis, no remaining activity
E292G
-
site-directed mutagenesis, 77.6% remaining activity
E292H
-
site-directed mutagenesis, 76% remaining activity
H293G
-
site-directed mutagenesis, no remaining activity
H293N
-
site-directed mutagenesis, no remaining activity
K107E/K252E
substitution does not alter catalytic efficiency with respect to the wild-type
V181A
78% of wild-type activity
V181L
26% of wild-type activity
V291G
-
site-directed mutagenesis, no remaining activity
Y180A
0.9% of wild-type activity
Y180F/N246A
substitution does not alter catalytic efficiency with respect to the wild-type
Y180P
less than 0.01% of wild-type activity
Y192A
21% of wild-type activity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55.9
melting temperature, N-terminal truncation mutant
56.4
melting temperature, wild-type
58.6
melting temperature, N-terminal truncation mutant, presence of myristoyl-CoA
59.5
melting temperature, wild-type, presence of myristoyl-CoA
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
acetonitrile, stable in 5% v/v
-
487764
dimethylsulfoxide, stable up to 40%
-
487778
ethanol, stable in 10% v/v
-
487764
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli
-
recombinant h28NMT from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged wild-type from Escherichia coli
-
recombinant His6-tagged Nef:NMT complex by nickel affinity chromatography, two proteins are able to remain associated through immunoprecipitation and
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in COS-7 cell, isoform 1 and 2
sequence comparisons
cloning of cDNA from liver mRNA, construction of 2 expression plasmids with ATG at position 28 and 211, respectively, termed h28NMT and h211NMT, functional expression in Escherichia coli and h28NMT in HEK 293 cells
-
codon-optimized Nef plasmid and the human NMT plasmid were cotransformed in BL21(DE3)
-
construction of expression plasmid encoding the enzyme, lacking the first 9 amino acid residues, fused to a enterokinase cleavage site and a polyhistidine tag, overexpression in Escherichia coli DH5alpha
-
expression as His-tagged protein in Escherichia coli
-
expression in Escherichia coli
expression of wild-type and mutants from Escherichia coli DH5alpha
-
gene cloned from cell culture and lymphocytes, in vitro translation of 2 different splice variants, DNA and amino acid sequence determination
-
overexpression in COS-7 cell, isoform 1 and 2
recombinant expression of His6-tagged Nef:NMT complex in Escherichia coli Codon Plus (DE-)-RIL cells
-
sequence comparisons
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacological inhibition of host cell N-myristoylation rapidly and completely prevents rhinoviral replication without inducing cytotoxicity. Inhibition of cotranslational myristoylation virus-encoded protein VP0 by inhibitor 1-(5-[3,4-difluoro-2-[2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethoxy]phenyl]-1-methyl-1H-indazol-3-yl)-N,N-dimethylmethanamine potently blocks a key step in viral capsid assembly, delivering low nanomolar antiviral activity against multiple rhinovirus strains, poliovirus and foot-and-mouth disease virus, and protection of cells against virus-induced killing, highlighting the potential of host myristoylation as a drug target in picornaviral infections
drug development
-
the enzyme is a target for drug design in the treatment of epilepsy
medicine
synthesis
-
recombinant expression of N-myristoylated proteins in Escherichia coli can be achieved by co-expressing N-myristoyltransferase and supplementing the growth medium with myristic acid. Undesired incorporation of the 12-carbon fatty acid lauric acid can also occur, leading to heterogeneous samples. A strategy for obtaining lauryl-free samples of myristoylated proteins in both rich and minimal media
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duronio, R.J.; Read, S.I.; Gordon, J.I.
Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
89
4129-4133
1992
Homo sapiens
Manually annotated by BRENDA team
Raju, R.V.S.; Datla, R.S.S.; Sharma, R.K.
Expression of human N-myristoyltransferase in Escherichia coli. Comparison with N-myristoyltransferases expressed in different tissues
Mol. Cell. Biochem.
155
69-76
1996
Homo sapiens
Manually annotated by BRENDA team
McIlhinney, R.A.J.; McGlone, K.
Immunocytochemical characterization and subcellular localization of human myristoyl-CoA: protein N-myristoyltransferase in HeLa cells
Exp. Cell Res.
223
348-356
1996
Homo sapiens
Manually annotated by BRENDA team
Young, K.; Egerton, M.; Camble, R.; White, A.; McIlhinney, R.A.J.
Immunochemical characterization of human N-myristoyltransferase: evidence for more than one form of the enzyme
Biochem. Soc. Trans.
25
S631
1997
Homo sapiens
Manually annotated by BRENDA team
Giang, D.K.; Cravatt, B.F.
A second mammalian N-myristoyltransferase
J. Biol. Chem.
273
6595-6598
1998
Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens, Mus musculus (O70310), Mus musculus (O70311), Mus musculus
Manually annotated by BRENDA team
Raju, R.V.S.; Datla, R.S.S.; Warrington, R.C.; Sharma, R.K.
Effects of L-histidine and its structural analogs on human N-myristoyltransferase activity and importance of EEVEH amino acid sequence for enzyme activity
Biochemistry
37
14928-14936
1998
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
McIlhinney, R.A.; Young, K.; Egerton, M.; Camble, R.; White, A.; Soloviev, M.
Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme
Biochem. J.
333
491-495
1998
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Pasha, M.K.; Dimmock, J.R.; Hollenberg, M.D.; Sharma, R.K.
Enhanced activity of human N-myristoyltransferase by dimethyl sulfoxide and related solvents in the presence of serine/threonine-containing peptide substrates
Biochem. Pharmacol.
64
1461-1467
2002
Homo sapiens
Manually annotated by BRENDA team
Selvakumar, P.; Lakshmikuttyamma, A.; Lawman, Z.; Bonham, K.; Dimmock, J.R.; Sharma, R.K.
Expression of methionine aminopeptidase 2,N-myristoyltransferase, and N-myristoyltransferase inhibitor protein 71 in HT29
Biochem. Biophys. Res. Commun.
322
1012-1017
2004
Homo sapiens
Manually annotated by BRENDA team
Hill, B.T.; Skowronski, J.
Human N-myristoyltransferases form stable complexes with lentiviral nef and other viral and cellular substrate proteins
J. Virol.
79
1133-1141
2005
Homo sapiens
Manually annotated by BRENDA team
Ma, H.H.; Yang, L.; Yang, X.Y.; Xu, Z.P.; Li, B.L.
Bacterial expression, purification, and in vitro N-myristoylation of fusion hepatitis B virus preS1 with the native-type N-terminus
Protein Expr. Purif.
27
49-54
2003
Homo sapiens
Manually annotated by BRENDA team
Selvakumar, P.; Lakshmikuttyamma, A.; Charavaryamath, C.; Singh, B.; Tuchek, J.; Sharma, R.K.
Expression of myristoyltransferase and its interacting proteins in epilepsy
Biochem. Biophys. Res. Commun.
335
1132-1139
2005
Bos taurus, Saccharomyces cerevisiae, Candida sp. (in: Saccharomycetales), Oryctolagus cuniculus, Dictyostelium sp., Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Breuer, S.; Gerlach, H.; Kolaric, B.; Urbanke, C.; Opitz, N.; Geyer, M.
Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef
Biochemistry
45
2339-2349
2006
Homo sapiens
Manually annotated by BRENDA team
Yamazaki, K.; Kaneko, Y.; Suwa, K.; Ebara, S.; Nakazawa, K.; Yasuno, K.
Synthesis of potent and selective inhibitors of Candida albicans N-myristoyltransferase based on the benzothiazole structure
Bioorg. Med. Chem.
13
2509-2522
2005
Candida albicans (P30418), Candida albicans, Homo sapiens (P30419)
Manually annotated by BRENDA team
Selvakumar, P.; Sharma, R.K.
Phosphorylation and dephosphorylation of human myristoyltransferase type 1
Can. J. Physiol. Pharmacol.
84
707-712
2006
Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Selvakumar, P.; Smith-Winsor, E.; Bonham, K.; Sharma, R.K.
N-Myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system
FEBS Lett.
580
2021-2026
2006
Homo sapiens
Manually annotated by BRENDA team
Selvakumar, P.; Sharma, R.K.
Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review)
Int. J. Mol. Med.
19
823-827
2007
Homo sapiens (O60551), Homo sapiens
Manually annotated by BRENDA team
Ducker, C.E.; Upson, J.J.; French, K.J.; Smith, C.D.
Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis
Mol. Cancer Res.
3
463-476
2005
Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Lu, Y.; Selvakumar, P.; Ali, K.; Shrivastav, A.; Bajaj, G.; Resch, L.; Griebel, R.; Fourney, D.; Meguro, K.; Sharma, R.K.
Expression of N-myristoyltransferase in human brain tumors
Neurochem. Res.
30
9-13
2005
Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Selvakumar, P.; Lakshmikuttyamma, A.; Shrivastav, A.; Das, S.B.; Dimmock, J.R.; Sharma, R.K.
Potential role of N-myristoyltransferase in cancer
Prog. Lipid Res.
46
1-36
2007
Oryctolagus cuniculus, Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens, Saccharomyces cerevisiae (P14743), Bos taurus (P31717), Bos taurus (Q9N181), Rattus norvegicus (Q8K1Q0)
Manually annotated by BRENDA team
Seaton, K.; Smith, C.
N-Myristoyltransferase isozymes exhibit differential specificity for human immunodeficiency virus type 1 Gag and Nef
J. Gen. Virol.
89
288-296
2008
Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Shrivastav, A.; Varma, S.; Lawman, Z.; Yang, S.H.; Ritchie, S.A.; Bonham, K.; Singh, S.M.; Saxena, A.; Sharma, R.K.
Requirement of N-myristoyltransferase 1 in the development of monocytic lineage
J. Immunol.
180
1019-1028
2008
Homo sapiens, Mus musculus (O70310), Mus musculus (O70311), Mus musculus
Manually annotated by BRENDA team
Lakshmikuttyamma, A.; Selvakumar, P.; Tuchek, J.; Sharma, R.
Myristoyltransferase and calcineurin: novel molecular therapeutic target for epilepsy
Prog. Neurobiol.
84
77-84
2008
Homo sapiens
Manually annotated by BRENDA team
Goncalves, V.; Brannigan, J.A.; Thinon, E.; Olaleye, T.O.; Serwa, R.; Lanzarone, S.; Wilkinson, A.J.; Tate, E.W.; Leatherbarrow, R.J.
A fluorescence-based assay for N-myristoyltransferase activity
Anal. Biochem.
421
342-344
2012
Homo sapiens
Manually annotated by BRENDA team
Morgan, C.R.; Miglionico, B.V.; Engen, J.R.
Effects of HIV-1 Nef on human N-myristoyltransferase 1
Biochemistry
50
3394-3403
2011
Homo sapiens
Manually annotated by BRENDA team
Kumar, S.; Singh, B.; Dimmock, J.R.; Sharma, R.K.
N-myristoyltransferase in the leukocytic development processes
Cell Tissue Res.
345
203-211
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Brand, S.; Cleghorn, L.A.; McElroy, S.P.; Robinson, D.A.; Smith, V.C.; Hallyburton, I.; Harrison, J.R.; Norcross, N.R.; Spinks, D.; Bayliss, T.; Norval, S.; Stojanovski, L.; Torrie, L.S.; Frearson, J.A.; Brenk, R.; Fairlamb, A.H.; Ferguson, M.A.; Read, K.D.; Wyatt, P.G.; Gilbert, I.H.
Discovery of a novel class of orally active trypanocidal N-myristoyltransferase inhibitors
J. Med. Chem.
55
140-152
2012
Homo sapiens, Trypanosoma brucei
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
Ohta, H.; Takamune, N.; Kishimoto, N.; Shoji, S.; Misumi, S.
N-Myristoyltransferase 1 enhances human immunodeficiency virus replication through regulation of viral RNA expression level
Biochem. Biophys. Res. Commun.
463
988-993
2015
Homo sapiens
Manually annotated by BRENDA team
Flamm, A.G.; Le Roux, A.L.; Mateos, B.; Diaz-Lobo, M.; Storch, B.; Breuker, K.; Konrat, R.; Pons, M.; Coudevylle, N.
N-Lauroylation during the expression of recombinant N-myristoylated proteins: implications and solutions
ChemBioChem
17
82-89
2016
Homo sapiens
Manually annotated by BRENDA team
Perinpanayagam, M.; Beauchamp, E.; Martin, D.; Sim, J.; Yap, M.; Berthiaume, L.
Regulation of co-and post-translational myristoylation of proteins during apoptosis: Interplay of N-myristoyltransferases and caspases
FASEB J.
27
811-821
2013
Homo sapiens
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
Kumar, S.; Sharma, R.
N-terminal region of the catalytic domain of human N-myristoyltransferase 1 acts as an inhibitory module
PLoS ONE
10
e0127661
2015
Homo sapiens (P30419), Homo sapiens
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
Soupene, E.; Kao, J.; Cheng, D.; Wang, D.; Greninger, A.; Knudsen, G.; DeRisi, J.; Kuypers, F.
Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA
J. Lipid Res.
57
288-298
2016
Homo sapiens (O60551), Homo sapiens
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
Mousnier, A.; Bell, A.S.; Swieboda, D.P.; Morales-Sanfrutos, J.; Perez-Dorado, I.; Brannigan, J.A.; Newman, J.; Ritzefeld, M.; Hutton, J.A.; Guedan, A.; Asfor, A.S.; Robinson, S.W.; Hopkins-Navratilova, I.; Wilkinson, A.J.; Johnston, S.L.; Leatherbarrow, R.J.; Tuthill, T.J.; Solari, R.; Tate, E.W.
Fragment-derived inhibitors of human N-myristoyltransferase block capsid assembly and replication of the common cold virus
Nat. Chem.
10
599-606
2018
Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Dian, C.; Perez-Dorado, I.; Riviere, F.; Asensio, T.; Legrand, P.; Ritzefeld, M.; Shen, M.; Cota, E.; Meinnel, T.; Tate, E.; Giglione, C.
High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
Nat. Commun.
11
1132
2020
Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Corbic Ramljak, I.; Stanger, J.; Real-Hohn, A.; Dreier, D.; Wimmer, L.; Redlberger-Fritz, M.; Fischl, W.; Klingel, K.; Mihovilovic, M.D.; Blaas, D.; Kowalski, H.
Cellular N-myristoyltransferases play a crucial picornavirus genus-specific role in viral assembly, virion maturation, and infectivity
PLoS Pathog.
14
e1007203
2018
Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team
Jacquier, M.; Kuriakose, S.; Bhardwaj, A.; Zhang, Y.; Shrivastav, A.; Portet, S.; Varma Shrivastav, S.
Investigation of novel regulation of N-myristoyltransferase by mammalian target of rapamycin in breast cancer cells
Sci. Rep.
8
12969
2018
Homo sapiens (P30419), Homo sapiens
Manually annotated by BRENDA team