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Enzyme Nomenclature
Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase
Word Map on EC 2.3.1.97
- 2.3.1.97
- myristate
-
n-myristoylation
-
antifungal
- albicans
-
co-translational
-
octapeptide
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14-carbon
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pp60src
-
nonmyristoylated
- benzofuran
- drug development
- molecular biology
- analysis
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.97
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RECOMMENDED NAME
GeneOntology No.
glycylpeptide N-tetradecanoyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
The enzyme from yeast is highly specific for tetradecanoyl-CoA, and highly specific for N-terminal glycine in oligopeptides containing serine in the 5-position. The enzyme from mammalian heart transfers acyl groups to a specific 51 kDa acceptor protein
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
requires alanine at position 5 of substrate peptides
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
ordered mechanism; peptide binding site
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
mechanism
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
interactions between enzyme and acyl-CoA and peptide substrates, formation of a high affinity reaction intermediate; mechanism
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
cooperativity between acyl-CoA and peptide binding sites
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
ordered bi bi mechanism; peptide binding site
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
myristoyl-CoA binding site; ordered bi bi mechanism; peptide binding site
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
PEST regions for recognition by clapains, putative regulatory enzymes
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
Glu290, Val-291 and His293 within conserved region EEVEH, are essential for catalysis
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
active site; binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate; kinetic analysis; ordered bi bi mechanism
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate; kinetic analysis; ordered bi bi mechanism
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate; detailed mechanism; myristoyl-CoA binding site; peptide binding site
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
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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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
N-myristoylation follows an ordered bi bi reaction mechanism in which myristoyl-CoA first binds to the NMT molecule inducing a conformational change and thus allowing for substrate binding followed by a direct nucleophilic addition-elimination reaction and the sequential release of CoA and the myristoyl-peptide
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
N-myristoylation follows an ordered bi bi reaction mechanism in which myristoyl-CoA first binds to the NMT molecule inducing a conformational change and thus allowing for substrate binding followed by a direct nucleophilic addition-elimination reaction and the sequential release of CoA and the myristoyl-peptide
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tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
N-myristoylation follows an ordered bi bi reaction mechanism in which myristoyl-CoA first binds to the NMT molecule inducing a conformational change and thus allowing for substrate binding followed by a direct nucleophilic addition-elimination reaction and the sequential release of CoA and the myristoyl-peptide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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addition
amide bond formation
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SYSTEMATIC NAME
IUBMB Comments
tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase
The enzyme from yeast is highly specific for tetradecanoyl-CoA, and highly specific for N-terminal glycine in oligopeptides containing serine in the 5-position. The enzyme from mammalian heart transfers acyl groups to a specific 51 kDa acceptor protein.
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CAS REGISTRY NUMBER
COMMENTARY
110071-61-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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487759, 487764, 487766, 487767, 487770, 487778, 657771, 659819, 660419, 671705, 672124, 673642, 735612, 735953, 736079
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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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
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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
evolution
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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
evolution
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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
evolution
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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
enzyme knockout leads to defective myelopoesis; enzyme knockout leads to defective myelopoesis
malfunction
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expression of isozyme NMT1 is reduced in lung inflammation and induced by Mannheimer hemolytica, probably due to increased enolase expression
malfunction
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NMT2 is not able to rescue N-myristoylation of proteins for the proper development of the embryos in NMT1-/- mice knockouts, the embryos die during early embryogenesis. Bone marrow cells taken from wild-type and heterozygous Nmt1-deficient mice and cultured in the presence of mouse macrophage colony-stimulating factor for differentiation into monocytes/macrophages develop in a different manner, overview
physiological function
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NMT1 is essential for the differentiation of U937 cells
physiological function
NMT1 is required in the development of monocytic lineage and essential for the early development of mouse embryo
physiological function
NMT catalyses the attachment of the 14-carbon saturated fatty acid, myristate, to the amino-terminal glycine residue of a subset of eukaryotic proteins that function in multiple cellular processes, including vesicular protein trafficking and signal transduction. In these pathways, N-myristoylation facilitates association of substrate proteins with membranes or the hydrophobic domains of other partner peptides. NMT function is essential for viability in all cell types tested to date; NMT function is essential for viability in host cells and in insect stages of the pathogenic protozoan parasite
physiological function
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N-myristoylation is a co-translational, irreversible addition of a fatty acyl moiety to the amino terminus of many eukaryotic cellular proteins. These myristoylated proteins in the cell have diverse biological functions such as signal transduction, cellular transformation and oncogensis
physiological function
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NMT plays a role in the regulation of neutrophil lifespan, overview. Myristoylated proteins play critical roles in protein-protein interactions, cell signaling and oncogenesis
physiological function
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myristoyl-CoA:protein N-myristoyltransferase is a ubiquitous enzyme in eukaryotes that catalyzes the co- and posttranslational transfer of a C14 saturated fatty acid (myristic acid) from myristoyl-CoA to the N-terminal glycine residue of target proteins
physiological function
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the HIV-1 accessory protein Nef is N-terminally myristoylated and this posttranslational modification is essential for Nef function in AIDS progression, Nef has no known catalytic activity but rather binds to a number of host-cell proteins. Transfer of a myristate group from myristoyl coenzyme A to Nef occurs cotranslationally and is catalyzed by human N-myristoyl transferase-1. Myristoylated Nef adopts a different tertiary and quaternary structure than non-myristoylated Nef, but conformational changes in Nef are no result of myristoylation, overview. NMT might chaperone Nef to the membrane and thereby protect the myristic acid group from the cytosol rather than Nef operating through a myristic acid switch mechanism
physiological function
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isozyme NMT1 is essential for growth and development, during which rapid cellular proliferation is required, in a variety of organisms. NMT1 is also reported to be elevated in many cancerous states, which also involve rapid cellular growth, albeit in an unwanted and uncontrolled manner. During the co-translational protein myristoylation, the initiator methionine at the N-terminus is removed by methionine aminopeptidase thus allowing the exposure of a glycine residue on an available myristoylation site. Myristoylation increases protein lipophilicity and controls the functioning of proteins by targeting them to specific localizations, promoting specific protein-protein and protein-lipid interactions and ligand-induced conformational changes. Roles of NMT in leukocytic differentiation processes and the roles of NMT1 in neutrophil apoptosis
physiological function
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isozyme NMT1 is essential for growth and development, during which rapid cellular proliferation is required, in a variety of organisms. NMT1 is also reported to be elevated in many cancerous states, which also involve rapid cellular growth, albeit in an unwanted and uncontrolled manner. During the co-translational protein myristoylation, the initiator methionine at the N-terminus is removed by methionine aminopeptidase thus allowing the exposure of a glycine residue on an available myristoylation site. Myristoylation increases protein lipophilicity and controls the functioning of proteins by targeting them to specific localizations, promoting specific protein-protein and protein-lipid interactions and ligand-induced conformational changes. Roles of NMT in leukocytic differentiation processes and the roles of NMT1 in neutrophil apoptosis
physiological function
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isozyme NMT1 is essential for growth and development, during which rapid cellular proliferation is required, in a variety of organisms. NMT1 is also reported to be elevated in many cancerous states, which also involve rapid cellular growth, albeit in an unwanted and uncontrolled manner. During the co-translational protein myristoylation, the initiator methionine at the N-terminus is removed by methionine aminopeptidase thus allowing the exposure of a glycine residue on an available myristoylation site. Myristoylation increases protein lipophilicity and controls the functioning of proteins by targeting them to specific localizations, promoting specific protein-protein and protein-lipid interactions and ligand-induced conformational changes. Roles of NMT in leukocytic differentiation processes and the roles of NMT1 in neutrophil apoptosis
physiological function
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expression of the Nmt gene is essential for viability. Partial repression of the gene reveals downstream effects of N-myristoylation on cell wall morphology
physiological function
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several RNA-binding proteins including ribosomal proteins, NMT isozymes, and hnRNP A2/B1 bind to NMT1, as mediated mainly by RNA. Only hRNP A2/B1 associates with NMT1 without mediation by RNA. Knockdown of hnRNP A2/B1 results in the enhancement of viral replication with an increase in the expression level of viral RNA in HIV-1-producing cells. Knockdown of NMT1 results in the attenuation of viral replication with the decrease in the expression level of viral RNA in HIV-1-producing cells. Overexpression of NMT1 induces the enhancement of viral replication with the increase in the expression level of the viral RNA
physiological function
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membrane protein calnexin interacts with N-myristoyltransferase 1 at the endoplasmic reticulum. NMT activity is not affected by presence of absence of calnexin
physiological function
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expression of NMT gene is essential for survival of Trypanosoma cruzi epimastigotes
physiological function
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expression of the Nmt gene is essential for viability. Partial repression of the gene reveals downstream effects of N-myristoylation on cell wall morphology
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physiological function
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NMT catalyses the attachment of the 14-carbon saturated fatty acid, myristate, to the amino-terminal glycine residue of a subset of eukaryotic proteins that function in multiple cellular processes, including vesicular protein trafficking and signal transduction. In these pathways, N-myristoylation facilitates association of substrate proteins with membranes or the hydrophobic domains of other partner peptides. NMT function is essential for viability in all cell types tested to date
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
11-(ethylthio)-undecanoyl-CoA + glycylpeptide
11-(ethylthio)-undecanoyl-glycylpeptide + CoA
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?
11-oxatetradecanoyl-CoA + G0alpha-hexapeptide
N-11-oxatetradecanoyl-G0alpha-hexapeptide + CoA
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-
-
-
?
11-phenylundecanoyl-CoA + glycylpeptide
11-phenylundecanoyl-glycylpeptide + CoA
-
-
-
-
?
13-oxatetradecanoyl-CoA + G0alpha-hexapeptide
N-13-oxatetradecanoyl-G0alpha-hexapeptide + CoA
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-
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?
6-oxatetradecanoyl-CoA + G0alpha-hexapeptide
N-6-oxatetradecanoyl-G0alpha-hexapeptide + CoA
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?
dodecanoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-dodecanoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
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?
lauryl-CoA + brain acid soluble protein 1
N-lauryl-brain acid soluble protein 1 + CoA
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N-laurylation of recombinant proteins in Escherichia coli may occur in minimal media
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?
lauryl-CoA + c-Src
N-lauryl-c-Src + CoA
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N-terminal region of c-Src, residues 1-185
N-laurylation of recombinant proteins in Escherichia coli may occur in minimal media
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?
myristoleoyl-CoA + glycylpeptide
N-myristoleoylglycylpeptide + CoA
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?
myristoyl-CoA + Arabidopsis thaliana protein CDPK6-derived peptide
N-myristoylated Arabidopsis thaliana protein CDPK6-derived peptide + CoA
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?
myristoyl-CoA + brain acid soluble protein 1
N-myristoyl-brain acid soluble protein 1 + CoA
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?
myristoyl-CoA + c-Src
N-myristoyl-c-Src + CoA
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N-terminal region of c-Src, residues 1-185
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?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
myristoyl-CoA + CAP5.5 peptide
N-myristoylglycyl-CAP5.5 peptide + CoA
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?
myristoyl-CoA + Fen kinase-derived peptide
N-myristoylated Fen kinase-derived peptide + CoA
plant protein peptide
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?
myristoyl-CoA + GAQLSTLSRV
myristoylglycyl-AQLSTLSRV + CoA
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?
myristoyl-CoA + Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val
N-myristoyl-Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val + CoA
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-
-
?
myristoyl-CoA + Gly-Ala-Arg-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Ala-Arg-Ala-Ala-Ala-Ala-Arg-Arg + CoA
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-
-
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?
myristoyl-CoA + Gly-Ala-Arg-Ala-Ser-Val-Leu-Ser
N-myristoyl-Gly-Ala-Arg-Ala-Ser-Val-Leu-Ser + CoA
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-
-
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?
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
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i.e. myristolated alanine-rich C-kinase substrate MARCKS
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?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala + CoA
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-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg + CoA
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Arg-Arg + CoA
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-
-
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?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
myristoyl-CoA + Gly-Asn-Ala-Pro-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Pro-Ala-Ala-Arg-Arg + CoA
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-
-
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?
myristoyl-CoA + Gly-Asn-Phe-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Phe-Ala-Ala-Ala-Arg-Arg + CoA
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-
-
-
?
myristoyl-CoA + Gly-Gln-Thr-Val-Thr-Thr-Pro-Leu
N-myristoyl-Gly-Gln-Thr-Val-Thr-Thr-Pro-Leu + CoA
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-
-
-
?
myristoyl-CoA + Gly-Leu-Tyr-Ala-Ser-Lys-Leu-Ser
N-myristoyl-Gly-Leu-Tyr-Ala-Ser-Lys-Leu-Ser + CoA
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-
-
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro
N-myristoyl-Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro + CoA
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-
-
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys + CoA
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-
-
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?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg + CoA
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Asp-Pro-Ser-Gln-Arg-Arg-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Asp-Pro-Ser-Gln-Arg-Arg-Arg + CoA
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pp60src-derived peptide
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-
?
myristoyl-CoA + HBV preS1
? + CoA
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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
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-
?
myristoyl-CoA + HBV preS1-HT
? + CoA
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fusion protein of hepatitis B virus preS1 with the native-type N-terminus and a His6-Tag fused to C-terminus
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-
?
myristoyl-CoA + HIV-1 Nef protein
?
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myristoylation results in conformational changes in HIV-1 Nef
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-
?
myristoyl-CoA + HIV-1 negative regulatory factor
N-myristoyl-HIV-1 negative regulatory factor + CoA
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-
-
-
?
myristoyl-CoA + M2 gene segment of reovirus type 3-derived peptide
N-myristoylated M2 gene segment of reovirus type 3-derived peptide + CoA
myristoyl-CoA + Nef
? + CoA
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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
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HIV-1 accessory protein Nef, usage of C-terminally 6xHis-tagged Nef SF2
-
-
?
myristoyl-CoA + peptide Hs pp60src(2-9)
CoA + N-myristoyl-peptideHs pp60src(2-9)
-
-
-
-
?
myristoyl-CoA + peptide pp60src(2-16)
CoA + N-myristoyl-peptideHs pp60src(2-16)
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sequence GSNKSKPKDASQRRR-NH2
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-
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myristoyl-CoA + Pr55gag-precursor-derived octapeptide
N-myristoylated Pr55gag-precursor-derived peptide + CoA
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peptide substrate is derived from human immunodeficiency virus
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?
myristoyl-CoA + tumor necrosis factor-derived peptide
N-myristoylated tumor necrosis factor-derived peptide + CoA
-
-
-
?
palmitoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-palmitoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
stearoyl-CoA + glycylpeptide
N-stearoylglycylpeptide + CoA
poor substrate
-
-
?
tetradecanoyl-CoA + GAAPSKIV-NH2
CoA + N-tetradecanoyl-GAAPSKIV-NH2
NMT catalyses the attachment of the 14C saturated fatty acid, myristate, to the N-terminal glycine residue of a protein. The fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the C-terminal lobe, substrate binding structure, overview
-
-
?
tetradecanoyl-CoA + GLTISKLFRR
CoA + N-tetradecanoyl-GLTISKLFRR
NMT catalyses the attachment of the 14C saturated fatty acid, myristate, to the N-terminal glycine residue of a protein. The fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the C-terminal lobe, substrate binding structure, overview
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
tetradecanoyl-CoA + glycyl-pp60cSrc
CoA + N-tetradecanoyl-glycyl-pp60cSrc
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycyl-pp60c Src
CoA + N-tetradecanoyl-glycyl-pp60c Src
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYVSRLFNRLFQKK(biotin)
CoA + N-tetradecanoyl-GLYVSRLFNRLFQKK(biotin)
NMT catalyses the attachment of the 14C saturated fatty acid, myristate, to the N-terminal glycine residue of a protein. The fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the C-terminal lobe, substrate binding structure, overview
-
-
?
tetradecanoyl-CoA + Plasmodium falciparum ADP ribosylation factor 1 peptide
CoA + N-myristoylated Plasmodium falciparum ADP ribosylation factor 1 peptide
-
model substrate, N-myristoylation of a glycine residue
-
-
ir
lauroyl-CoA + glycylpeptide
N-lauroylglycylpeptide + CoA
low activity
-
-
?
myristoleoyl-CoA + CAP5.5
N-myristoleoyl-CAP5.5 + CoA
acceptor is biotin-tagged cytoskeleton-associated protein 5.5
-
-
?
myristoleoyl-CoA + CAP5.5
N-myristoleoyl-CAP5.5 + CoA
acceptor is biotin-tagged cytoskeleton-associated protein 5.5
-
-
?
myristoyl-CoA + ARF peptide
CoA + N-myristoyl-ARF peptide
C-terminally biotinylated ARF peptide, i.e. GLYVSRLFNRLFQKK(Biotin)-NH2, substrate binding structures, overview
-
-
?
myristoyl-CoA + ARF peptide
CoA + N-myristoyl-ARF peptide
C-terminally biotinylated ARF peptide, i.e. GLYVSRLFNRLFQKK(Biotin)-NH2, substrate binding structures, overview
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
-
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
-
-
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
-
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
-
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
-
i.e. Gly-Asn-Ala-Ala-Ala-Ala-Lys-Lys-Arg-Arg
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
cAMP-dependent protein kinase-derived peptide
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg + CoA
-
pp60src-derived peptide
-
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg + CoA
-
pp60src-derived peptide
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg + CoA
-
pp60src-derived peptide
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
substrate specificity
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
altered fatty acid chain length
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
specific for myristoyl-CoA
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
essential for growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
altered fatty acid chain length
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is possibly regulated by calpains in vivo
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
overview peptides and proteins
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
the enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
N-myristoylation is a process of covalent irreversible protein modification that promotes association of proteins with membranes
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
cross talk between enzyme and protein substrate
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
the enzyme is essential for viability in Leishmania, constitutively expressed in all parasite stages
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
overview peptides and proteins
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
diverse protein substrates, protein biosynthesis
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
N-myristoyltransferase 1 is not essential for the viability of mammalian cells but is required for development, likely because it is the principal N-myristoyltransferase in early embryogenesis
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
cAMP-dependent protein kinase-derived peptide
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
p60src-derived peptides
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
p60src-derived peptides
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by CoA-derivatives of hydroxytetradecanoic acids, azidoaromatic analogues of myristic acid, omega-nitrocarboxylic acids, halogen- and haloaromatic analogues of myristic acid and, with low activity, by dicarboxylic fatty acids
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
stereochemical requirements
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
stereochemical requirements
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
biotinylated peptides
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
altered fatty acid chain length
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-peptides can compete with myristoyl-CoA for the binding site
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by oxygen or sulfur mono-substituted analogs
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by phenyl-, furyl-, thienyl-, acylohexyl-substituted fatty acids
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by unsaturated fatty acids
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by oxygen or sulfur di-substituted analogs
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for uncharged amino acid at position 2 of peptide chain, no peptides with bulky hydrophobic side chains at position 2, broad spectrum of amino acids in position 3, overview
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
overview peptides and proteins
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
-
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for myristoyl-CoA
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for myristoyl-CoA
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
p60src-derived peptides
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
p60src-derived peptides
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
altered fatty acid chain length
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by oxygen or sulfur mono-substituted analogs
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by unsaturated fatty acids
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
altered fatty acid chain length
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
the enzyme is essential for both life cycle stages of Trypanosoma brucei
-
-
?
myristoyl-CoA + M2 gene segment of reovirus type 3-derived peptide
N-myristoylated M2 gene segment of reovirus type 3-derived peptide + CoA
-
-
-
-
?
myristoyl-CoA + M2 gene segment of reovirus type 3-derived peptide
N-myristoylated M2 gene segment of reovirus type 3-derived peptide + CoA
-
i.e. Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
retina enzyme
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
hexadecapeptide from N-terminus
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
decapeptide, best substrate
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
-
-
?
myristoyl-CoA + peptide CAP5.5
CoA + N-myristoyl-peptide CAP5.5
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein
-
-
?
myristoyl-CoA + peptide CAP5.5
CoA + N-myristoyl-peptide CAP5.5
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein
-
-
?
myristoyl-CoA + peptide CAP5.5
CoA + N-myristoyl-peptide CAP5.5
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein
-
-
?
myristoyl-CoA + protein
?
-
proteins involved in metabolic regulation, e.g. catalytic subunit of protein kinase A and G protein alpha subunit
-
-
-
myristoyl-CoA + protein
?
-
natural protein substrates are: catalytic subunit of cAMP-dependent protein kinase, p60src, phosphatases, e.g. calcineurin B, transmembrane signalling proteins, e.g. alpha-subunits of heterotrimeric G proteins, gag polyprotein precursors of several retroviruses, capsid proteins of some parvoviruses and picornaviruses
-
-
ir
n-decanoyl-CoA + glycylpeptide
N-decanoylglycylpeptide + CoA
low activity
-
-
?
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
poor substrate
-
-
?
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
poor substrate
-
-
?
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
no activity
-
-
-
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
no activity
-
-
-
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
-
-
-
?
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
poor substrate
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
i.e. myristoyl-CoA, NMT2 has approximately 5fold higher catalytic efficiency for the myristoylation of Nef than NMT1
-
-
?
tetradecanoyl-CoA + glycyl-pp60c-Src
CoA + N-tetradecanoyl-glycyl-pp60c-Src
-
-
-
-
?
tetradecanoyl-CoA + glycyl-pp60c-Src
CoA + N-tetradecanoyl-glycyl-pp60c-Src
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
-
i.e. myristoyl-CoA, the enzyme attaches the fatty acid to a glycine at the N-terminus of proteins
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
-
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
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
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
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
-
-
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
-
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
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
covalent attachment of the myristoyl group, generally to the N-terminal glycine residue of proteins. N-myristoylation occurs absolutely on an exposed N-terminal glycine and on a general consesus motif of GXXXS/T, where X is any amino acid
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
posttranslational transfer of a C14 saturated fatty acid (myristic acid) from myristoyl-CoA to the N-terminal glycine residue of target proteins
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
transfer of a C14 saturated fatty acid (myristic acid) from myristoyl-CoA to the N-terminal glycine residue of target proteins
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
NMT catalyses the attachment of the 14C saturated fatty acid, myristate, to the N-terminal glycine residue of a subset of eukaryotic proteins that function in multiple cellular processes, including vesicular protein trafficking and signal transduction
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
covalent attachment of the myristoyl group, generally to the N-terminal glycine residue of proteins. N-myristoylation occurs absolutely on an exposed N-terminal glycine and on a general consesus motif of GXXXS/T, where X is any amino acid
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
-
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
covalent attachment of the myristoyl group, generally to the N-terminal glycine residue of proteins. N-myristoylation occurs absolutely on an exposed N-terminal glycine and on a general consesus motif of GXXXS/T, where X is any amino acid
-
-
?
additional information
?
-
-
ablating NMT1 is more effective in inhibiting tumor growth than is ablation of NMT2
-
-
-
additional information
?
-
-
NMT1 is critical for tumor cell proliferation. Ablating NMT1 is more effective in inhibiting tumor growth than is ablation of NMT2
-
-
-
additional information
?
-
-
isozyme NMT1 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
-
strong interaction of NMT2 with caspase-3 with a probable major role in the cellular regulation of NMT2, caspase-3 interaction with NMT2 is stronger than with NMT1. The cellular regulation of NMT1 and NMT2 is mediated by two different signaling molecules, m-calpain and caspase, respectively, overview. Protein-protein interaction of NMT forms and p53
-
-
-
additional information
?
-
N-myristoyltransferase isozymes exhibit differential specificity for human immunodeficiency virus type 1 Gag and Nef, overview
-
-
-
additional information
?
-
N-myristoyltransferase isozymes exhibit differential specificity for human immunodeficiency virus type 1 Gag and Nef, overview
-
-
-
additional information
?
-
-
development of a robust sensitive fluorescence-based assay method to study the enzymatic activity of NMT1 and NMT2 based on detection of CoA by 7-diethylamino-3-(4-maleimido-phenyl)-4-methylcoumarin, overview
-
-
-
additional information
?
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein, with myristoyl-CoA
-
-
-
additional information
?
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein, with myristoyl-CoA
-
-
-
additional information
?
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein, with myristoyl-CoA
-
-
-
additional information
?
-
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein, with myristoyl-CoA
-
-
-
additional information
?
-
the fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the carboxy-terminal lobe, substrate binding structure, overview
-
-
-
additional information
?
-
-
the fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the carboxy-terminal lobe, substrate binding structure, overview
-
-
-
additional information
?
-
the fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the carboxy-terminal lobe, substrate binding structure, overview
-
-
-
additional information
?
-
isozyme NMT1 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
isozyme NMT1 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
isozyme NMT2 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
isozyme NMT2 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
active site structure, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes the cotranslational irreversible addition of a fatty acyl moiety to the N-terminus of proteins
-
-
-
additional information
?
-
-
presence of approximately 60 putative N-myristoylated proteins encoded by the Trypanosoma brucei genome
-
-
-
additional information
?
-
N-myristoylation of the synthetic peptide CAP5.5, derived from the N-terminus of the Trypanosoma brucei CAP5.5 protein, with myristoyl-CoA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + HBV preS1
? + CoA
-
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 + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
-
retina enzyme
-
?
tetradecanoyl-CoA + glycyl-HIV1 Gag protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Gag protein N-terminal peptide
O60551, P30419
-
-
-
?
tetradecanoyl-CoA + glycyl-HIV1 Nef protein N-terminal peptide
CoA + N-tetradecanoyl-glycyl-HIV1 Nef protein N-terminal peptide
O60551, P30419
-
-
-
?
tetradecanoyl-CoA + glycyl-pp60cSrc
CoA + N-tetradecanoyl-glycyl-pp60cSrc
O70310, O70311
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycyl-pp60c Src
CoA + N-tetradecanoyl-glycyl-pp60c Src
O70310, O70311
i.e. myristoyl-CoA
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
Q9LTR9
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
Q9LTR9
essential for growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is possibly regulated by calpains in vivo
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
the enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
N-myristoylation is a process of covalent irreversible protein modification that promotes association of proteins with membranes
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
Q9GPZ4
the enzyme is essential for viability in Leishmania, constitutively expressed in all parasite stages
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
diverse protein substrates, protein biosynthesis
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
N-myristoyltransferase 1 is not essential for the viability of mammalian cells but is required for development, likely because it is the principal N-myristoyltransferase in early embryogenesis
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
the enzyme is essential for both life cycle stages of Trypanosoma brucei
-
-
?
myristoyl-CoA + protein
?
-
proteins involved in metabolic regulation, e.g. catalytic subunit of protein kinase A and G protein alpha subunit
-
-
-
myristoyl-CoA + protein
?
-
natural protein substrates are: catalytic subunit of cAMP-dependent protein kinase, p60src, phosphatases, e.g. calcineurin B, transmembrane signalling proteins, e.g. alpha-subunits of heterotrimeric G proteins, gag polyprotein precursors of several retroviruses, capsid proteins of some parvoviruses and picornaviruses
-
-
ir
tetradecanoyl-CoA + glycyl-pp60c-Src
CoA + N-tetradecanoyl-glycyl-pp60c-Src
-
-
-
-
?
tetradecanoyl-CoA + glycyl-pp60c-Src
CoA + N-tetradecanoyl-glycyl-pp60c-Src
-
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
-
i.e. myristoyl-CoA, the enzyme attaches the fatty acid to a glycine at the N-terminus of proteins
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
-
-
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
covalent attachment of the myristoyl group, generally to the N-terminal glycine residue of proteins. N-myristoylation occurs absolutely on an exposed N-terminal glycine and on a general consesus motif of GXXXS/T, where X is any amino acid
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
posttranslational transfer of a C14 saturated fatty acid (myristic acid) from myristoyl-CoA to the N-terminal glycine residue of target proteins
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
D0AB09
NMT catalyses the attachment of the 14C saturated fatty acid, myristate, to the N-terminal glycine residue of a subset of eukaryotic proteins that function in multiple cellular processes, including vesicular protein trafficking and signal transduction
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
covalent attachment of the myristoyl group, generally to the N-terminal glycine residue of proteins. N-myristoylation occurs absolutely on an exposed N-terminal glycine and on a general consesus motif of GXXXS/T, where X is any amino acid
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
-
covalent attachment of the myristoyl group, generally to the N-terminal glycine residue of proteins. N-myristoylation occurs absolutely on an exposed N-terminal glycine and on a general consesus motif of GXXXS/T, where X is any amino acid
-
-
?
additional information
?
-
-
ablating NMT1 is more effective in inhibiting tumor growth than is ablation of NMT2
-
-
-
additional information
?
-
-
NMT1 is critical for tumor cell proliferation. Ablating NMT1 is more effective in inhibiting tumor growth than is ablation of NMT2
-
-
-
additional information
?
-
-
isozyme NMT1 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
-
strong interaction of NMT2 with caspase-3 with a probable major role in the cellular regulation of NMT2, caspase-3 interaction with NMT2 is stronger than with NMT1. The cellular regulation of NMT1 and NMT2 is mediated by two different signaling molecules, m-calpain and caspase, respectively, overview. Protein-protein interaction of NMT forms and p53
-
-
-
additional information
?
-
O70310
isozyme NMT1 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
O70311
isozyme NMT1 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
O70310
isozyme NMT2 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
O70311
isozyme NMT2 catalyzes myristoylation of various proteins crucial in signal transduction, cellular transformation, and oncogenesis
-
-
-
additional information
?
-
-
the enzyme catalyzes the cotranslational irreversible addition of a fatty acyl moiety to the N-terminus of proteins
-
-
-
additional information
?
-
-
presence of approximately 60 putative N-myristoylated proteins encoded by the Trypanosoma brucei genome
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
negligible effect on enzyme activity by calmodulin and Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclopentanecarboxamide
-
IC50: 0.000015 mM
(1R,3S)-N-{2-[(cyclopeanthylcarbonyl)amino]-benzothiazol-6-yl}-3-[(2-naphthylmethyl) amino] cyclohexanecarboxamide
-
competitive with the substrate peptide and non-competitive with myristoyl-CoA. IC50: 0.49 nM
(1S,3R)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: above 0.00001 mM
(1S,3R)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclopentanecarboxamide
-
IC50: 0.000011mM
(2S)-N-(2-cyclohexylethyl)-2-[[N-([3-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetyl)-L-seryl]amino]heptanamide
(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
(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
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-acetyl-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
-
2,6-dichloro-4-(1,2,3,4-tetrahydroisoquinolin-5-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2,6-dichloro-4-(2-piperazin-1-ylpyridin-4-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-benzenesulfonamide
-
-
2,6-dichloro-4-(isoquinolin-5-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
IC50 value against amastigotes 0.00015 microM
2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,5-dimethyl-3-isobutyl-1H-pyrazol-4-yl)benzenesulfonamide
-
inhibits the enzyme and is fungicidal under partially repressive nmt conditions
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
2,6-dichloro-4-[6-(piperazin-1-yl)pyridin-3-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2-(acetylamino)-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.01 mM
2-(benzylamino)-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.01 mM
2-([2-[(2,3-difluorophenoxy)methyl]-3-methyl-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([2-[(2,4-difluorophenoxy)methyl]-3-methyl-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([2-[(2-fluorophenoxy)methyl]-3-methyl-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([2-[(3-fluorophenoxy)methyl]-3-methyl-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([2-[(4-chlorophenoxy)methyl]-3-methyl-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([2-[(4-fluorophenoxy)methyl]-3-methyl-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([3-methyl-2-[(phenylsulfanyl)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-([[(1R,3S)-3-[[(5-chloro-7-methylnaphthalen-2-yl)methyl]amino]cyclohexyl]acetyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-([[trans-4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-amino-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.01 mM
2-oxo-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
-
-
2-[(2-methylpropanoyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
2-[(3-methyl-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-yl)methoxy]benzonitrile
-
-
2-[(4-methoxybenzyl)amino]-5,5-dimethyl-4,7-dihydro-5H-thieno[2,3-c]pyran-3-carbonitrile
-
-
2-[(cyclobutylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
2-[(cyclohexanecarbonyl)amino]-N-[(2-naphthylmethyl)amino]ethyl-benzothiazole-6-carboxamide
2-[(cyclohexylcarbonyl)amino]-1-methyl-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1H-benzimidazole-5-carboxamide
-
IC50: above 0.1 mM
2-[(cyclohexylcarbonyl)amino]-1-methyl-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1H-benzimidazole-6-carboxamide
-
IC50: above 0.1 mM
2-[(cyclohexylcarbonyl)amino]-N-(3-[[(naphthalen-2-ylmethyl)amino]methyl]benzyl)-1,3-benzothiazole-6-carboxamide
-
IC50: 0.0019 mM
2-[(cyclohexylcarbonyl)amino]-N-(4-[[(naphthalen-2-ylmethyl)amino]methyl]benzyl)-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.1 mM
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-5-carboxamide
-
IC50: 0.0068 mM
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-7-carboxamide
-
IC50: 0.001 mM
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzoxazole-5-carboxamide
-
IC50: 0.0011 mM
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzoxazole-6-carboxamide
-
IC50: 0.00029 mM
2-[(cyclohexylcarbonyl)amino]-N-[3-[(naphthalen-2-ylmethyl)amino]propyl]-1,3-benzothiazole-6-carboxamide
2-[(cyclohexylcarbonyl)amino]-N-[4-[(naphthalen-2-ylmethyl)amino]butyl]-1,3-benzothiazole-6-carboxamide
2-[(cyclohexylcarbonyl)amino]-N-[5-[(naphthalen-2-ylmethyl)amino]pentyl]-1,3-benzothiazole-6-carboxamide
2-[(cyclohexylmethyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.001 mM
2-[(cyclopentylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-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
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-[([(1R,3S)-3-[(1H-indol-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
2-[[(2,5-dimethoxyphenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
2-[[(2-chloropyridin-3-yl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
2-[[(3,4-dichlorophenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
2-[[(4-chlorophenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
2-[[3-methyl-2-(2-phenylethyl)-1-benzofuran-4-yl]oxy]-N-(pyridin-3-ylmethyl)ethanamine
-
-
2-[[3-methyl-2-(phenoxymethyl)-1-benzofuran-4-yl]oxy]-N-(pyridin-3-ylmethyl)ethanamine
-
-
3',5'-dichloro-4'-[(1,3,5-trimethyl-1H-pyrazol-4-yl)sulfamoyl]biphenyl-3-carboxamide
-
-
3,5-dichloro-3'-[(4-methylpiperazin-1-yl)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
-
-
3,5-dichloro-3'-[(diethylamino)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
-
-
3,5-dichloro-4'-[(4-methylpiperazin-1-yl)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
-
-
3,5-dichloro-4'-[(diethylamino)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
-
-
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
3-[[3-methyl-2-[[2,3,4-tris(fluoranyl)phenoxy]methyl]-1-benzofuran-4-yl]oxy]-N-(pyridin-3-ylmethyl)propan-1-amine
-
i.e. Ro-09-4879
4-(1H-pyrazol-1-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
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
4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5-dihydroxybenzamide
4-(4-chloro-2-[5-[(trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl]phenoxy)piperidine
-
high affinity inhibitor of Leishmania donovani, does not not display significant selectivity for Leishmania donovania over the human enzyme. Compound does not display any macrophage toxicity up to 0.09 mM
4-bromo-2,6-dichloro-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-benzenesulfonamide
-
-
4-bromo-N-(2-methylpropyl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzamide
-
-
4-bromo-N-methyl-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
4-methoxy-2,3,6-trimethyl-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
4-methoxy-2,3,6-trimethyl-N-[(1,3,5-trimethyl-1H-pyrazol-4-yl)methyl]benzenesulfonamide
-
-
4-[(3-methyl-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-yl)methoxy]benzonitrile
-
-
6-(2-methyl-1,3-thiazol-4-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-(benzylamino)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-(morpholin-4-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-([2-[4-(propan-2-yl)piperazin-1-yl]ethyl]amino)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[(1H-indol-5-ylmethyl)amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[2-(4-methylpiperazin-1-yl)ethylamino]pyridine-3-sulfonic acid (1,3,5-trimethyl-1H-pyrazol-4-yl)amide
-
-
6-[3-(piperazin-1-yl)piperidin-1-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[3-(piperazin-1-yl)pyrrolidin-1-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(1-methylpiperidin-4-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(1H-imidazol-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(4-benzylpiperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(4-methylpiperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(4-phenylpiperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(morpholin-4-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(piperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[2-(piperidin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[3-(dimethylamino)propyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
6-[[4-[(dimethylamino)methyl]benzyl](methyl)amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
-
-
Ala-Leu-Tyr-Ala-Ser-Lys-Leu-Ser
-
competitve against peptide substrate Gly-Leu-Tyr-Ala-Ser-Lys-Leu-Ser
-
benzyl-{3-[2-(2-ethoxymethyl-benzofuran-5-ylmethoxymethyl)-3-methyl-benzofuran-4-yloxy]-propyl}-amine
-
-
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
ethyl 3-(1-methylethyl)-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-cyclopropyl-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-ethyl-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-methyl-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 4-(but-3-yn-1-ylsulfanyl)-6-(1-hydroxyethyl)quinoline-3-carboxylate
-
-
ethyl 4-[2-hydroxy-3-(isopropylamino)propoxy]-3-methyl-1-benzofuran-2-carboxylate
-
-
ethyl 4-[2-hydroxy-3-[(2-methylpropyl)amino]propoxy]-3-methyl-1-benzofuran-2-carboxylate
-
-
ethyl 4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 4-[3-(tert-butylamino)propoxy]-3-methyl-1-benzofuran-2-carboxylate
-
-
ethyl 4-[3-[(2,2-dimethylpropyl)amino]-2-hydroxypropoxy]-3-methyl-1-benzofuran-2-carboxylate
-
-
ethyl 4-[[5-(tert-butylamino)pentyl]oxy]-3-methyl-1-benzofuran-2-carboxylate
-
-
HIV1 Nef protein N-terminal peptide
Nef peptide acts as a competitive inhibitor for the myristoylation of Gag; Nef peptide acts as a competitive inhibitor for the myristoylation of Gag
-
Inhibitor protein from bovine brain
-
located in the membrane fraction, heat-stable, monomeric, 71 kDa
-
m-calpain
-
enzyme is inactivated by cleavage, protease is specific for PEST regions, i.e. regions rich in proline, glutamic acid, serine and threonine, calpain-inhibitor calpastatin protects
-
N-(1-propyl-3,5-dimethyl-1H-pyrazol-4-yl)-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-(3,4-dimethyl-1,2-oxazol-5-yl)-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-(3,5-dimethyl-1,2-oxazol-4-yl)-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-(3,5-dimethyl-1-propyl-1H-pyrazol-4-yl)-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-(3,5-dimethyl-1H-pyrazol-4-yl)-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-(6-[[N-(biphenyl-4-ylmethyl)-b-alanyl]amino]-1,3-benzothiazol-2-yl)cyclopentanecarboxamide
-
IC50: 0.00016 mM
N-(6-[[N-(naphthalen-2-ylmethyl)-b-alanyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
N-(6-[[N-(naphthalen-2-ylmethyl)glycyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
N-(imidazo[1,2-a]pyridin-3-yl)-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
N-[(3-methyl-4-[2-[(pyridin-3-ylmethyl)amino]ethoxy]-1-benzofuran-2-yl)oxy]aniline
-
-
N-[1,3-dimethyl-5-(morpholin-4-yl)-1H-pyrazol-4-yl]-4-methoxy-2,3,6-trimethylbenzenesulfonamide
-
-
N-[2-chloro-5-[(3S,4R)-1-[4-(4-chlorophenyl)-3-hydroxybutanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]phenyl]-2-(4-fluorophenyl)acetamide
N-[2-[(2-methylpropanoyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.0000033 mM
N-[2-[(cyclobutylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.0000023 mM
N-[2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.0000081 mM
N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.0000012 mM
N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[[(4-phenylcyclohexa-1,5-dien-1-yl)methyl]amino]cyclohexanecarboxamide
-
IC50: 0.00013 mM
N-[2-[(cyclopropylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.0000024 mM
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.01 mM
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-(propanoylamino)-1,3-benzothiazole-6-carboxamide
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-([[4-(trifluoromethyl)phenyl]carbonyl]amino)-1,3-benzothiazole-6-carboxamide
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(phenylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyrazin-2-ylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyridin-2-ylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyridin-2-ylmethyl)amino]-1,3-benzothiazole-6-carboxamide
-
IC50: above 0.01 mM
N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide
N-[6-([3-[(naphthalen-2-ylmethyl)amino]azetidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
N-[6-([3-[(naphthalen-2-ylmethyl)amino]piperidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
N-[6-([3-[(naphthalen-2-ylmethyl)amino]pyrrolidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
N-[6-([4-[(naphthalen-2-ylmethyl)amino]butanoyl]amino)-1,3-benzothiazol-2-yl]cyclopentanecarboxamide
-
IC50: 0.000015 mM
N-[6-([4-[(naphthalen-2-ylmethyl)amino]piperidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
N-[6-[(4-[[(naphthalen-2-ylmethyl)amino]methyl]piperidin-1-yl)carbonyl]-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
Octapeptide inhibitors with hydrophobic amino acid in position 2
-
-
-
tert-butyl 4-[2-([5-[(1,3,5-trimethyl-1H-pyrazol-4-yl)sulfamoyl]pyridin-2-yl]amino)ethyl]piperazine-1-carboxylate
-
-
tert-butyl [6-([2-[(naphthalen-2-ylmethyl)amino]ethyl]carbamoyl)-1,3-benzothiazol-2-yl]carbamate
-
IC50: above 0.01 mM
trans-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.000034 mM
[4-[3-(benzylamino)propoxy]-3-methyl-1-benzofuran-2-yl](1-methyl-1H-imidazol-2-yl)methanone
{3-[2-(1H-imidazol-2-yl)-3-methyl-benzofuran-4-yloxy]-propyl}-pyridin-3-ylmethyl-amine
-
-
-
{3-[2-(2,3-difluoro-phenoxymethyl)-3-methyl-benzofuran-4-yloxy]-propyl}-pyridin-3-ylmethyl-amine
-
-
{3-[2-(2-ethoxymethyl-benzofuran-5-yloxymethyl)-3-methyl-benzofuran-4-yloxy]-propyl}-pyridin-3-ylmethyl-amine
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
IC50: 0.00000049 mM
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(2S)-N-(2-cyclohexylethyl)-2-[[N-([3-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetyl)-L-seryl]amino]heptanamide
-
-
(2S)-N-(2-cyclohexylethyl)-2-[[N-([3-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetyl)-L-seryl]amino]heptanamide
-
(2S)-N-(2-cyclohexylethyl)-2-[[N-([3-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetyl)-L-seryl]amino]heptanamide
-
(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-[(3R,4S)-3-(hydroxymethyl)-4-(4-methoxyphenyl)pyrrolidin-1-yl]butan-1-one
-
-
(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-[(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
;
(3R)-3-amino-4-(4-chlorophenyl)-1-[(3S,4R)-3-(4-chlorophenyl)-4-(hydroxymethyl)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
-
(3R)-3-amino-4-(4-chlorophenyl)-1-[(3S,4R)-3-(4-chlorophenyl)-4-(hydroxymethyl)pyrrolidin-1-yl]butan-1-one
-
(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
-
-
(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
-
-
(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
-
-
(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
-
-
(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
-
-
(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
-
-
(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
-
-
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-(2,4-difluorobenzyl)azetidine-3-carboxamide
-
-
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-(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-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-[(5-methylpyrazin-2-yl)methyl]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-chloro-2-[[2-(dimethylamino)ethyl]amino]pyrimidin-4-yl)-N-[(5-methylpyrazin-2-yl)methyl]azetidine-3-carboxamide
-
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
-
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
IC50 value against promastigotes 0.0227 microM, against amastigotes 0.0073 microM
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
inhibits growth of Trypanosoma cruzi epimastigotes with EC50 of 6.9 microM, but is about 1000fold less potent than in Trypanosma brucei
2-(4-fluorophenyl)-N-[3-(piperidin-4-yl)-1H-indol-5-yl]acetamide
;
2-(4-fluorophenyl)-N-[3-(piperidin-4-yl)-1H-indol-5-yl]acetamide
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-([[(1R,3S)-3-[[(5-chloro-7-methylnaphthalen-2-yl)methyl]amino]cyclohexyl]acetyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[(1R,3S)-3-[[(5-chloro-7-methylnaphthalen-2-yl)methyl]amino]cyclohexyl]acetyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
2-([[(1R,3S)-3-[[(5-chloro-7-methylnaphthalen-2-yl)methyl]amino]cyclohexyl]acetyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[trans-4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-([[trans-4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
2-([[trans-4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
2-[(2-methylpropanoyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: 0.000046 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
-
IC50: 0.000028 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
-
IC50: 0.0000344 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
-
IC50: 0.00011 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
-
IC50: 0.000074 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
-
IC50: 0.0003 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
-
IC50: 0.000023 mM
2-[(cyclopentylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
32% inhibition at 0.01 mM
2-[([(1R,3S)-3-[(1-benzofuran-5-ylmethyl)amino]cyclohexyl]acetyl)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
-
2-[([(1R,3S)-3-[(1-benzofuran-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
2-[([(1R,3S)-3-[(1H-indol-5-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[[(2,5-dimethoxyphenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
-
IC50: 0.00031 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
-
IC50: above 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
-
IC50: above 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
-
IC50: above 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
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
;
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
-
-
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
-
3-(methyl[6-methyl-2-[methyl(1-methylpiperidin-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]amino)propanenitrile
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5-dihydroxybenzamide
-
-
4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5-dihydroxybenzamide
-
4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5-dihydroxybenzamide
-
-
5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
;
5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
-
-
5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
-
5-chloro-2-[[4-(3,5-difluorophenyl)piperidin-1-yl]methyl]-1-methyl-1H-benzimidazole
-
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
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-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]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
-
-
cis-N-1,3-benzothiazol-2-yl-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-1,3-benzothiazol-2-yl-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-1,3-benzothiazol-2-yl-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-1,3-benzothiazol-2-yl-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-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
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
factor NIP71
-
bovine brain inhibitor protein; strong inhibition in a concentration dependent manner, noncompetitive
-
heat shock cognate protein 70
involved in NMT1 regulation, overview; involved in NMT1 regulation, overview
-
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-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
peptidomimetic inhibitor
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
peptidomimetic inhibitor
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
peptidomimetic inhibitor
N-(6-[[N-(naphthalen-2-ylmethyl)-b-alanyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
IC50: 0.00018 mM
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
-
IC50: 0.0023 mM
N-(6-[[N-(naphthalen-2-ylmethyl)glycyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
8% inhibition at 0.01 mM
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
;
N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
-
-
N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
-
N-[(3R)-1-(N-methylglycyl)pyrrolidin-3-yl]-2-(trifluoromethyl)benzamide
-
N-[2-chloro-5-[(3S,4R)-1-[4-(4-chlorophenyl)-3-hydroxybutanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]phenyl]-2-(4-fluorophenyl)acetamide
-
inhibitor shows good selectiviy over the human enzyme
N-[2-chloro-5-[(3S,4R)-1-[4-(4-chlorophenyl)-3-hydroxybutanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]phenyl]-2-(4-fluorophenyl)acetamide
inhibitor shows good selectiviy over the human enzyme
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-(propanoylamino)-1,3-benzothiazole-6-carboxamide
-
IC50: 0.00013 mM
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
-
IC50: above 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
-
IC50: 0.00016 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
-
IC50: 0.00073 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
-
IC50: above 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-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide
-
inhibitor shows good selectiviy over the human enzyme
N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide
inhibitor shows good selectiviy over the human enzyme
N-[6-([3-[(naphthalen-2-ylmethyl)amino]azetidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
-
IC50: 0.000065 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
-
IC50: 0.00021 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
-
IC50: 0.00019 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
-
IC50: 0.0005 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
-
IC50: 0.000026 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
;
N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
-
-
N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
-
N-[[3'-(6,7-dihydro[1,3]thiazolo[5,4-c]pyridin-5(4H)-ylmethyl)biphenyl-3-yl]methyl]-2-(pyridin-3-yl)ethanamine
-
S-(2-oxo)pentadecyl-CoA
i.e. NHM, a non-hydrolysable myristoyl-CoA analogue, binding structure analysis, overview; i.e. NHM, a non-hydrolysable myristoyl-CoA analogue, binding structure, overview
SC-58272
-
peptidomimetic derived from the N-terminal sequence of the substrate ADP-ribosylation factor-2, i.e. Arf2p
[4-[3-(benzylamino)propoxy]-3-methyl-1-benzofuran-2-yl](1-methyl-1H-imidazol-2-yl)methanone
-
-
[4-[3-(benzylamino)propoxy]-3-methyl-1-benzofuran-2-yl](1-methyl-1H-imidazol-2-yl)methanone
-
[4-[3-(benzylamino)propoxy]-3-methyl-1-benzofuran-2-yl](1-methyl-1H-imidazol-2-yl)methanone
-
additional information
-
inhibitor design and three-dimensional quantitative structure-activity relationship analysis, modelling, detailed overview
-
additional information
-
inhibitor design and development, overview
-
additional information
development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview; development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview
-
additional information
development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview; development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview
-
additional information
ligand binding structure-function analysis for drug design, overview
-
additional information
-
ligand binding structure-function analysis for drug design, overview
-
additional information
-
development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview
-
additional information
-
binding mode, structure-activity relationship and selectivity of inhibitors, overview. The enzyme is a target for rational inhibitor design, modelling of inhibitor docking, overview
-
additional information
binding mode, structure-activity relationship and selectivity of inhibitors, overview. The enzyme is a target for rational inhibitor design, modelling of inhibitor docking, overview
-
additional information
-
development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview
-
additional information
development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview
-
additional information
-
NMT inhibitors: screening, synthesis, and structural characterization of their binding mode, overview
-
additional information
-
overview: inhibition by glycylpeptides with varying amino acids at positions 2 to 8
-
additional information
-
inhibitor design and development, overview
-
additional information
-
binding mode, structure-activity relationship and selectivity of inhibitors, overview. The enzyme is a target for rational inhibitor design, modelling of inhibitor docking, overview
-
additional information
development of specific anti-protozoan inhibitors against NMT, specificity over the human isozymes, component screening, structure-activity relationships, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
8.5fold increase in activity with Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg, 10fold with Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg and 7fold increase with Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys; activation mechanism; activation requires a serine in the peptide substrate
N-myristoyltransferase activator NAF45
-
absolutely required for activity of brain enzyme isoforms, maximal 3-4fold activation; from brain, 45 kDa protein; increase of Km for peptide substrates
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0205
Arabidopsis thaliana protein CDPK6-derived peptide
recombinant enzyme
-
0.022
CAP5.5
-
pH not specified in the publication, temperature not specified in the publication
-
0.016
Gly-(diaminobutyrate-gamma-NH2-4-azido, 3-iodosalicylamide)-Ala-Ala-Ser-Ala-Arg-Arg
-
-
0.0008
myristoleoyl-CoA
-
pH not specified in the publication, temperature not specified in the publication
0.00571
peptide pp60src(2-16)
-
pH and temperature not specified in the publication
-
0.0144
HIV-1 negative regulatory factor
-
N-terminal truncation mutant, pH 7.5, 25°C
-
0.196
HIV1 Gag protein N-terminal peptide
pH 7.4, 37°C, isozyme NMT2; pH 7.4, 37°C, isozyme NMT2
-
0.33
HIV1 Gag protein N-terminal peptide
pH 7.4, 37°C, isozyme NMT1; pH 7.4, 37°C, isozyme NMT1
-
0.0015
HIV1 Nef protein N-terminal peptide
pH 7.4, 37°C, isozyme NMT2; pH 7.4, 37°C, isozyme NMT2
-
0.011
HIV1 Nef protein N-terminal peptide
pH 7.4, 37°C, isozyme NMT1; pH 7.4, 37°C, isozyme NMT1
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview fatty acid analogs with various substituents
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview fatty acid analogs with various substituents
-
additional information
additional information
-
Km for several protein-derived peptides
-
additional information
additional information
Km for several protein-derived peptides
-
additional information
additional information
NMT1 and NMT2 have 30 and 130fold lower Km values for Nef than Gag, respectively. Michaelis-Menten kinetics, and kinetic modelling of isozymes, overview; NMT1 and NMT2 have 30 and 130fold lower Km values for Nef than Gag, respectively. Michaelis-Menten kinetics, and kinetic modelling of isozymes, overview
-
additional information
additional information
NMT1 and NMT2 have 30 and 130fold lower Km values for Nef than Gag, respectively. Michaelis-Menten kinetics, and kinetic modelling of isozymes, overview; NMT1 and NMT2 have 30 and 130fold lower Km values for Nef than Gag, respectively. Michaelis-Menten kinetics, and kinetic modelling of isozymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.107
HIV1 Gag protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT2; pH 7.4, 37°C, isozyme NMT2
-
0.265
HIV1 Gag protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT1; pH 7.4, 37°C, isozyme NMT1
-
0.032
HIV1 Nef protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT2; pH 7.4, 37°C, isozyme NMT2
-
0.052
HIV1 Nef protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT1; pH 7.4, 37°C, isozyme NMT1
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.98
HIV1 Gag protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT2; pH 7.4, 37°C, isozyme NMT2
6367
1
HIV1 Gag protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT1; pH 7.4, 37°C, isozyme NMT1
6367
4.9
HIV1 Nef protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT1; pH 7.4, 37°C, isozyme NMT1
5436
23.6
HIV1 Nef protein N-terminal peptide
Homo sapiens
O60551, P30419
pH 7.4, 37°C, isozyme NMT2; pH 7.4, 37°C, isozyme NMT2
5436
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0263
1-[(diethylamino)methyl]naphthalen-2-ol
-
pH and temperature not specified in the publication
0.0000063
2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
pH not specified in the publication, temperature not specified in the publication
0.0000025 - 0.0000228
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
0.0264
2-[(4-methoxybenzyl)amino]-5,5-dimethyl-4,7-dihydro-5H-thieno[2,3-c]pyran-3-carbonitrile
-
pH and temperature not specified in the publication
0.0116
3-butyl-4-(but-3-yn-1-ylsulfanyl)-6-methoxy-2-methylquinoline
-
pH and temperature not specified in the publication
0.1
3-butyl-6-methoxy-2-methyl-4-[(2-phenylethyl)sulfanyl]quinoline
-
above, pH and temperature not specified in the publication
0.0216
3-[(2-bromo-3-butyl-6-methoxyquinolin-4-yl)sulfanyl]propanenitrile
-
pH and temperature not specified in the publication
0.0174
3-[(3-butyl-6-methoxy-2-methylquinolin-4-yl)sulfanyl]propan-1-ol
-
pH and temperature not specified in the publication
0.0029
3-[(3-butyl-6-methoxy-2-methylquinolin-4-yl)sulfanyl]propanenitrile
-
pH and temperature not specified in the publication
0.00246
3-[(3-butyl-6-methoxyquinolin-4-yl)sulfanyl]propanenitrile
-
pH and temperature not specified in the publication
0.00323
3-[(3-ethyl-6-methoxy-2-methylquinolin-4-yl)sulfanyl]propanenitrile
-
pH and temperature not specified in the publication
0.1
3-[(6-methoxy-2-methylquinolin-4-yl)sulfanyl]propanenitrile
-
above, pH and temperature not specified in the publication
0.00001
4-(4-chloro-2-[5-[(trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl]phenoxy)piperidine
-
pH not specified in the publication, temperature not specified in the publication
0.0352
4-[(3-butyl-6-methoxy-2-methylquinolin-4-yl)sulfanyl]butanenitrile
-
pH and temperature not specified in the publication
0.0114
6-ethyl-3-(trifluoromethyl)-2,3-dihydro-1,4-benzoxathiine 4,4-dioxide
-
pH and temperature not specified in the publication
0.1
ethyl 4-(but-3-yn-1-ylsulfanyl)-6-(1-hydroxyethyl)quinoline-3-carboxylate
-
above, pH and temperature not specified in the publication
0.0109
ethyl 4-(but-3-yn-1-ylsulfanyl)-6-chloroquinoline-3-carboxylate
-
pH and temperature not specified in the publication
0.00777
ethyl 4-(but-3-yn-1-ylsulfanyl)-6-fluoroquinoline-3-carboxylate
-
pH and temperature not specified in the publication
0.00697
ethyl 4-(but-3-yn-1-ylsulfanyl)-6-methylquinoline-3-carboxylate
-
pH and temperature not specified in the publication
0.1
ethyl 4-[(2-cyanoethyl)amino]quinoline-3-carboxylate
-
above, pH and temperature not specified in the publication
0.0606
ethyl 4-[(2-cyanoethyl)sulfanyl]-2-ethylquinoline-3-carboxylate
-
pH and temperature not specified in the publication
0.02437
ethyl 4-[(2-cyanoethyl)sulfanyl]-2-methylquinoline-3-carboxylate
-
above, pH and temperature not specified in the publication
0.1
ethyl 4-[(2-cyanoethyl)sulfanyl]-2-propylquinoline-3-carboxylate
-
above, pH and temperature not specified in the publication
0.0424
ethyl 4-[(2-cyanoethyl)sulfanyl]-6-methoxyquinoline-3-carboxylate
-
pH and temperature not specified in the publication
0.02442
ethyl 4-[(2-cyanoethyl)sulfanyl]quinoline-3-carboxylate
-
pH and temperature not specified in the publication
0.1
ethyl 6-acetyl-4-(but-3-yn-1-ylsulfanyl)quinoline-3-carboxylate
-
above, pH and temperature not specified in the publication
0.1
[(3-butyl-6-methoxy-2-methylquinolin-4-yl)sulfanyl]acetonitrile
-
above, pH and temperature not specified in the publication
0.0000025
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
pH not specified in the publication, temperature not specified in the publication
0.0000228
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
-
pH 7.4, 30°C
additional information
additional information
-
overview: Ki values for glycylpeptides with varying amino acids at positions 2 to 5
-
additional information
additional information
-
Ki of several mutants for S-(2-oxo)-pentadecyl-CoA at 24 and 37°C
-
additional information
additional information
competitive inhibition kinetics of HIV1 Gag and Nef protein N-terminal peptides, overview; competitive inhibition kinetics of HIV1 Gag and Nef protein N-terminal peptides, overview
-
additional information
additional information
competitive inhibition kinetics of HIV1 Gag and Nef protein N-terminal peptides, overview; competitive inhibition kinetics of HIV1 Gag and Nef protein N-terminal peptides, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000049
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.00000049 mM
0.000015
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclopentanecarboxamide
Candida albicans
-
IC50: 0.000015 mM
0.00000049
(1R,3S)-N-{2-[(cyclopeanthylcarbonyl)amino]-benzothiazol-6-yl}-3-[(2-naphthylmethyl) amino] cyclohexanecarboxamide
Candida albicans
-
competitive with the substrate peptide and non-competitive with myristoyl-CoA. IC50: 0.49 nM
0.00001
(1S,3R)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: above 0.00001 mM
0.000011
(1S,3R)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclopentanecarboxamide
Candida albicans
-
IC50: 0.000011mM
0.0086
1-acetyl-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0043
2,6-dichloro-4-(1,2,3,4-tetrahydroisoquinolin-5-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.000002
2,6-dichloro-4-(2-piperazin-1-ylpyridin-4-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.049
2,6-dichloro-4-(isoquinolin-5-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.000012
2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,5-dimethyl-3-isobutyl-1H-pyrazol-4-yl)benzenesulfonamide
Aspergillus fumigatus
-
pH not specified in the publication, temperature not specified in the publication
0.0000137 - 0.000023
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
0.00029
2,6-dichloro-4-[6-(piperazin-1-yl)pyridin-3-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.001
2,6-dichloro-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.01
2-(acetylamino)-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.01
2-(benzylamino)-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.01
2-amino-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.0033
2-oxo-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-1,2,3,4-tetrahydroquinoline-6-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.000046
2-[(2-methylpropanoyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.000046 mM
0.000028
2-[(cyclobutylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.000028 mM
0.0000344
2-[(cyclohexanecarbonyl)amino]-N-[(2-naphthylmethyl)amino]ethyl-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.0000344 mM
0.1
2-[(cyclohexylcarbonyl)amino]-1-methyl-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1H-benzimidazole-5-carboxamide
Candida albicans
-
IC50: above 0.1 mM
0.1
2-[(cyclohexylcarbonyl)amino]-1-methyl-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1H-benzimidazole-6-carboxamide
Candida albicans
-
IC50: above 0.1 mM
0.0019
2-[(cyclohexylcarbonyl)amino]-N-(3-[[(naphthalen-2-ylmethyl)amino]methyl]benzyl)-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.0019 mM
0.1
2-[(cyclohexylcarbonyl)amino]-N-(4-[[(naphthalen-2-ylmethyl)amino]methyl]benzyl)-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.1 mM
0.0068
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-5-carboxamide
Candida albicans
-
IC50: 0.0068 mM
0.001
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-7-carboxamide
Candida albicans
-
IC50: 0.001 mM
0.0011
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzoxazole-5-carboxamide
Candida albicans
-
IC50: 0.0011 mM
0.00029
2-[(cyclohexylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzoxazole-6-carboxamide
Candida albicans
-
IC50: 0.00029 mM
0.00011
2-[(cyclohexylcarbonyl)amino]-N-[3-[(naphthalen-2-ylmethyl)amino]propyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.00011 mM
0.000074
2-[(cyclohexylcarbonyl)amino]-N-[4-[(naphthalen-2-ylmethyl)amino]butyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.000074 mM
0.0003
2-[(cyclohexylcarbonyl)amino]-N-[5-[(naphthalen-2-ylmethyl)amino]pentyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.0003 mM
0.001
2-[(cyclohexylmethyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.001 mM
0.000023
2-[(cyclopentylcarbonyl)amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.000023 mM
0.00031
2-[[(2,5-dimethoxyphenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.00031 mM
0.01
2-[[(2-chloropyridin-3-yl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.01
2-[[(3,4-dichlorophenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.01
2-[[(4-chlorophenyl)carbonyl]amino]-N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.0009
3',5'-dichloro-4'-[(1,3,5-trimethyl-1H-pyrazol-4-yl)sulfamoyl]biphenyl-3-carboxamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.000005
3,5-dichloro-3'-[(4-methylpiperazin-1-yl)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00002
3,5-dichloro-3'-[(diethylamino)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0012
3,5-dichloro-4'-[(4-methylpiperazin-1-yl)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.011
3,5-dichloro-4'-[(diethylamino)methyl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)biphenyl-4-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.028
3-cyano-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0048
4-(1H-pyrazol-1-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.000034
4-bromo-2,6-dichloro-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)-benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.1
4-bromo-N-[(1,3,5-trimethyl-1H-pyrazol-4-yl)methyl]benzenesulfonamide
Trypanosoma brucei
-
above, pH 7.4, 22°C
0.032
4-cyano-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.1
4-[(4-bromophenoxy)methyl]-1,3,5-trimethyl-1H-pyrazole
Trypanosoma brucei
-
above, pH 7.4, 22°C
0.042
4-[[(4-bromophenyl)sulfonyl]methyl]-1,3,5-trimethyl-1H-pyrazole
Trypanosoma brucei
-
pH 7.4, 22°C
0.012
6-(2-methyl-1,3-thiazol-4-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0013
6-(benzylamino)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0019
6-(morpholin-4-yl)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.001
6-([2-[4-(propan-2-yl)piperazin-1-yl]ethyl]amino)-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.026
6-chloro-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00033
6-[(1H-indol-5-ylmethyl)amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00014
6-[2-(4-methylpiperazin-1-yl)ethylamino]pyridine-3-sulfonic acid (1,3,5-trimethyl-1H-pyrazol-4-yl)amide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00003
6-[3-(piperazin-1-yl)piperidin-1-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00011
6-[3-(piperazin-1-yl)pyrrolidin-1-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00003
6-[[2-(1-methylpiperidin-4-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0013
6-[[2-(1H-imidazol-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.01
6-[[2-(4-benzylpiperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00011
6-[[2-(4-methylpiperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.001
6-[[2-(4-phenylpiperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.038
6-[[2-(morpholin-4-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.001
6-[[2-(piperazin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.014
6-[[2-(piperidin-1-yl)ethyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0021
6-[[3-(dimethylamino)propyl]amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.00036
6-[[4-[(dimethylamino)methyl]benzyl](methyl)amino]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)pyridine-3-sulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.012
N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.1
N-(4-bromobenzyl)-1,3,5-trimethyl-1H-pyrazol-4-amine
Trypanosoma brucei
-
above, pH 7.4, 22°C
0.1
N-(4-bromophenyl)-1,3,5-trimethyl-1H-pyrazole-4-carboxamide
Trypanosoma brucei
-
above, pH 7.4, 22°C
0.1
N-(4-bromophenyl)-1,3,5-trimethyl-1H-pyrazole-4-sulfonamide
Trypanosoma brucei
-
above, pH 7.4, 22°C
0.00016
N-(6-[[N-(biphenyl-4-ylmethyl)-b-alanyl]amino]-1,3-benzothiazol-2-yl)cyclopentanecarboxamide
Candida albicans
-
IC50: 0.00016 mM
0.00018
N-(6-[[N-(naphthalen-2-ylmethyl)-b-alanyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
Candida albicans
-
IC50: 0.00018 mM
0.0023
N-(6-[[N-(naphthalen-2-ylmethyl)glycyl]amino]-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0023 mM
0.000059
N-[2-chloro-5-[(3S,4R)-1-[4-(4-chlorophenyl)-3-hydroxybutanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]phenyl]-2-(4-fluorophenyl)acetamide
Leishmania donovani
-
pH not specified in the publication, temperature not specified in the publication
0.0000033
N-[2-[(2-methylpropanoyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0000033 mM
0.0000023
N-[2-[(cyclobutylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0000023 mM
0.0000081
N-[2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0000081 mM
0.0000012
N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0000012 mM
0.00013
N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[[(4-phenylcyclohexa-1,5-dien-1-yl)methyl]amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.00013 mM
0.0000024
N-[2-[(cyclopropylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0000024 mM
0.01
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.00013
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-(propanoylamino)-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.00013 mM
0.01
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-([[4-(trifluoromethyl)phenyl]carbonyl]amino)-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.00016
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(phenylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.00016 mM
0.00073
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyrazin-2-ylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: 0.00073 mM
0.01
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyridin-2-ylcarbonyl)amino]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.01
N-[2-[(naphthalen-2-ylmethyl)amino]ethyl]-2-[(pyridin-2-ylmethyl)amino]-1,3-benzothiazole-6-carboxamide
Candida albicans
-
IC50: above 0.01 mM
0.0028
N-[4-[(1,3,5-trimethyl-1H-pyrazol-4-yl)sulfamoyl]phenyl]acetamide
Trypanosoma brucei
-
pH 7.4, 22°C
0.0000016
N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide
Leishmania donovani
-
pH not specified in the publication, temperature not specified in the publication
0.000065
N-[6-([3-[(naphthalen-2-ylmethyl)amino]azetidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.000065 mM
0.00021
N-[6-([3-[(naphthalen-2-ylmethyl)amino]piperidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.00021 mM
0.00019
N-[6-([3-[(naphthalen-2-ylmethyl)amino]pyrrolidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.00019 mM
0.000015
N-[6-([4-[(naphthalen-2-ylmethyl)amino]butanoyl]amino)-1,3-benzothiazol-2-yl]cyclopentanecarboxamide
Candida albicans
-
IC50: 0.000015 mM
0.0005
N-[6-([4-[(naphthalen-2-ylmethyl)amino]piperidin-1-yl]carbonyl)-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.0005 mM
0.000026
N-[6-[(4-[[(naphthalen-2-ylmethyl)amino]methyl]piperidin-1-yl)carbonyl]-1,3-benzothiazol-2-yl]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.000026 mM
0.01
tert-butyl 4-[2-([5-[(1,3,5-trimethyl-1H-pyrazol-4-yl)sulfamoyl]pyridin-2-yl]amino)ethyl]piperazine-1-carboxylate
Trypanosoma brucei
-
pH 7.4, 22°C
0.01
tert-butyl [6-([2-[(naphthalen-2-ylmethyl)amino]ethyl]carbamoyl)-1,3-benzothiazol-2-yl]carbamate
Candida albicans
-
IC50: above 0.01 mM
0.000034
trans-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
Candida albicans
-
IC50: 0.000034 mM
0.0000137
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Homo sapiens
-
pH 7.9-8.0, 25°C, isozyme NMT1
0.0000144
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Homo sapiens
-
pH 7.9-8.0, 25°C, isozyme NMT2
0.000023
2,6-dichloro-4-[2-(piperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide
Aspergillus fumigatus
-
pH not specified in the publication, temperature not specified in the publication
0.000024
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Leishmania donovani
-
pH not specified in the publication, temperature not specified in the publication
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
0.00068
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Plasmodium vivax
A5K1A2
pH not specified in the publication, temperature not specified in the publication
0.0243
N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.000349
N-(11-aminoundecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Homo sapiens
-
pH 7.9-8.0, 25°C, isozyme NMT1
0.000513
N-(11-aminoundecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
Homo sapiens
-
pH 7.9-8.0, 25°C, isozyme NMT2
additional information
additional information
Homo sapiens
O60551
IC50 values of different inhibitors, overview; IC50 values of different inhibitors, overview
-
additional information
additional information
Homo sapiens
P30419
IC50 values of different inhibitors, overview; IC50 values of different inhibitors, overview
-
additional information
additional information
Leishmania donovani
-
IC50 values of different inhibitors, overview
-
additional information
additional information
Plasmodium falciparum
-
IC50 values of different inhibitors, overview
-
additional information
additional information
Plasmodium falciparum
Q8ILW6
IC50 values of different inhibitors, overview
-
additional information
additional information
Trypanosoma brucei
D0A003
IC50 values of different inhibitors, overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
assay development, ELISA with biotinylated peptide substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
about half-maximal activity above pH 9.0 and below pH 7.0, inactive at pH 6.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
elevated NMT activity and higher protein expressions. Higher NMT activity in WHO grade I malignancy, compared with others of higher WHO grades; elevated NMT activity and higher protein expressions. Higher NMT activity in WHO grade I malignancy, compared with others of higher WHO grades
-
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
-
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
-
overexpression of NMT2. Caspase-3 interacts with NMT2
-
N-myristoyltransferase 1 is not essential for the viability of mammalian cells but is required for development, likely because it is the principal N-myristoyltransferase in early embryogenesis
-
increased in the myocardium of ischemia-reperfusion rat model myocardium. Rats with mild or no detectable Parkinson syndrome features on rotenone show slight but insignificantly increased activity. Rats with moderately severe Parkinson syndrome features have higher level of NMT activity, which is borderline significant compared to controls. Rats with severe PS features had the highest NMT activity which is significantly greater compared to controls and to the rats with equivocal or no motor slowing
additional information
-
bone marrow cells taken from wild-type and heterozygous Nmt1-deficient mice and cultured in the presence of mouse macrophage colony-stimulating factor for differentiation into monocytes/macrophages develop in a different manner, overview
-
NMT activity is observed to be 5fold higher in bone marrow cells from rats with colonic cancer than in controls, and shows also differential localization
-
high NMT1 expression in neutrophils from the necrotic areas in inflamed lungs
-
NMT activity is observed to be 3fold higher in peripheral blood mononuclear cells from rats with colonic cancer than in controls, and shows also differential localization
additional information
-
2 different splicing variants occur in rat tissues, the 62 kDa variant is abundant in most tissues, the 42 kDa variant occurs in brain and stomach
additional information
-
in rats with colonic tumors, NMT1 expression and activity are significantly elevated in peripheral blood mononuclear cells and bone marrow cells compared with those in normal rats
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme interacts with calnexin at the endoplasmic reticulum
-
predominantly cytosolic isoform NMT2 relocalizes to membranes when cleaved by caspases
-
NMT activity remains associated with the transmembrane fraction even after extensive washings
-
caspase-mediated cleavage of the predominantly membrane bound isoform NMT1 removes a polybasic domain stretch and leads to a cytosolic relocalization
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
-
1 * 43000, active low MW form generated by proteolysis during storage, SDS-PAGE
48000
50000
55000
60000
additional information
48000
-
1 * 48000, splice variant 2 from in vitro translation, also recombinant enzyme from Escherichia coli, SDS-PAGE
additional information
-
enzyme forms multiple high molecular weight aggregates of fully active monomers
additional information
amino acid sequence alignment and comparison, isoforms 1 and 2; amino acid sequence alignment and comparison, isoforms 1 and 2
additional information
amino acid sequence alignment and comparison, isoforms 1 and 2; amino acid sequence alignment and comparison, isoforms 1 and 2
additional information
amino acid sequence alignment and comparison, isoforms 1 and 2; amino acid sequence alignment and comparison, isoforms 1 and 2
additional information
amino acid sequence alignment and comparison, isoforms 1 and 2; amino acid sequence alignment and comparison, isoforms 1 and 2
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
-
1 * 43000, active low MW form generated by proteolysis during storage, SDS-PAGE; 1 * 60000, SDS-PAGE
monomer
-
1 * 47000-49000, active form after storage at 4°C, SDS-PAGE; 1 * 60000, SDS-PAGE
monomer
-
1 * 48000, recombinant h211NMT, SDS-PAGE; 1 * 60000, recombinant h28NMT, SDS-PAGE; 1 * 62000, native from, SDS-PAGE
monomer
1 * 49000-68000, several forms of isoform 1, SDS-PAGE; 1 * 65000, isoform 2, SDS-PAGE
monomer
-
1 * 48000, splice variant 2 from in vitro translation, also recombinant enzyme from Escherichia coli, SDS-PAGE; 1 * 62000-63000, splice variant 1, SDS-PAGE
monomer
-
1 * 48000, splice variant 2, SDS-PAGE; 1 * 62000-63000, splice variant 1, SDS-PAGE
additional information
-
2 interconvertable forms of 60000 and 47000 Da, both catalytically active, formation of multimeric complexes, molecular weight reduction is not only due to proteolysis but has a possible regulatory role in vivo
additional information
-
NMT consists of saddle-shaped beta-sheet flanked by alpha helices and exhibits a pseudo twofold symmetry with regions corresponding to the N- and C-terminal portions of the enzyme. The N-terminal half forms the myristoyl-CoA-binding site, whereas the C-terminal half forms the major portion of the peptide-binding site
additional information
-
three-dimensional model formation using the cyrstal structure and homology modeling method, and energy minimization and molecular dynamics simulations
additional information
-
NMT consists of saddle-shaped beta-sheet flanked by alpha helices and exhibits a pseudo twofold symmetry with regions corresponding to the N- and C-terminal portions of the enzyme. The N-terminal half forms the myristoyl-CoA-binding site, whereas the C-terminal half forms the major portion of the peptide-binding site
additional information
three-dimensional model formation using the cyrstal structure and homology modeling method, and energy minimization and molecular dynamics simulations
additional information
-
NMT consists of saddle-shaped beta-sheet flanked by alpha helices and exhibits a pseudo twofold symmetry with regions corresponding to the N- and C-terminal portions of the enzyme. The N-terminal half forms the myristoyl-CoA-binding site, whereas the C-terminal half forms the major portion of the peptide-binding site
additional information
-
three-dimensional model formation using the cyrstal structure and homology modeling method, and energy minimization and molecular dynamics simulations
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors 2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,5-dimethyl-3-isobutyl-1H-pyrazol-4-yl)benzenesulfonamide and 2,6-dichloro-4-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-N-(1,3,5-trimethyl-1H-pyrazol-4-yl)benzenesulfonamide binding in the peptide substrate pocket
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ternary complex of NMT with S-(2-oxo)pentadecyl-CoA, a myristoyl-CoA analogue cofactor, and synthetic inhibitor Ro-09-4879, 3-[[3-methyl-2-[[2,3,4-tris(fluoranyl)phenoxy]methyl]-1-benzofuran-4-yl]oxy]-N-(pyridin-3-ylmethyl)propan-1-amine, to a resolution of 2.1 A
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ternary complex formation incubation of protein, 60 mg/ml, with 5fold molar of myristoyl-CoA and inhibitor SC-58272 for a few hours, hanging drop at 4°C, from 0.2 M ammonium acetate, 50 mM HEPES, pH 7.5, 10-12% polyethylene glycol 3350, 2-3 weeks, crystal structure determination by X-ray diffraction analysis
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in complex with inhibitor 4-(4-chloro-2-[5-[(trimethyl-1H-pyrazol-4-yl)methyl]-1,3,4-oxadiazol-2-yl]phenoxy)piperidine. The basic piperidine moiety forms a polar interaction with the carboxylate of the C-terminal residue, Leu421 and a water-mediated interaction with Tyr92, mimicking the N-terminus of substrate peptides. In addition, the trimethyl pyrazole substituent forms pi-pi and polar interactions with Phe90 and Ser330, respectively
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purified recombinant enzyme in complex with the non-hydrolysable substrate analogue S-(2-oxo)pentadecyl-CoA, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement method; purified recombinant His-tagged NMT in complex with the non-hydrolysable substrate analogue S-(2-oxo)pentadecyl-CoA, hanging drop vapour diffusion method, mixing of 0.00125 ml of protein solution containing 8 mg/ml protein in 50 mM Tris, pH 8.0, 50 mM NaCl , with 0.00125 l of reservoir solution containing 0.6 M lithium chloride, 20% w/v PEG 6000, 4% v/v 1,4-butanediol in 0.5 M sodium citrate, pH 4.0, equilibration against 0.8 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement
in complex with inhibitors N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide and N-[2-chloro-5-[(3S,4R)-1-[4-(4-chlorophenyl)-3-hydroxybutanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]phenyl]-2-(4-fluorophenyl)acetamide. The para-fluorophenyl acetamide in ortho-position to the chlorine atom in compound N-[5-[(4R)-1-[(3R)-3-amino-4-(4-chlorophenyl)butanoyl]-4-(hydroxymethyl)pyrrolidin-3-yl]-2-chlorophenyl]-2-(4-fluorophenyl)acetamide significantly improves potency. This could potentially introduce hydrogen bonding between the acetamide carbonyl and Tyr345 and Asn376 and allow the compound to extend into a hydrophobic pocket
in complex with both myristoyl-CoA and inhibitor N-(10-aminodecanoyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide. The inhibitor sits in the peptide-binding pocket, and mimics the key recognition elements involved in binding the parent peptide
hanging drops over a solution of 0.1 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.4, 20°C, 20% polyethylene glycol 4000, protein 25 mg/ml, a few days, structure determination and analysis by X-ray diffraction of binary and ternary complexes of enzyme, peptide substrate or myristoyl-CoA and inhibitor
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58.6
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melting temperature, N-terminal truncation mutant, presence of myristoyl-CoA
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, conversion of 60000 Da form into 47000 Da form, loss of 30% activity within 10 days
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4°C, conversion of 60000 Da form into 47000 Da form, activity is stable over several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged recombinant wild-type and mutants from Escherichia coli
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partial
partially
recombinant enzyme from Escherichia coli strain BL21(DE3); recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) pRareS by metal affinity chromatography and gel filtration, removal of the His-tag by cleavage with HRV 3C protease
recombinant from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli
recombinant His6-tagged Nef:NMT complex by nickel affinity chromatography, two proteins are able to remain associated through immunoprecipitation and
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recombinant His6-tagged NMT2 from Escherichia coli by nickel affinity chromatography to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cardiac muscle enzyme, expression in Escherichia coli, DNA and amino acid sequence determination
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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
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codon-optimized Nef plasmid and the human NMT plasmid were cotransformed in BL21(DE3)
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construction of expression plasmid encoding the enzyme, lacking the first 8 amino acid residues, fused to a enterokinase cleavage site and a polyhistidine tag, expression in Escherichia coli DH5alpha, cDNA from spleen
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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
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DNA and amino acid sequence determination and analysis, overexpression of the His-tagged NMT in Escherichia coli strain BL21(DE3) pRareS; overexpression in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
expression in Escherichia coli JM101, coexpression of each of the 4 homologous rat alpha subunits of the signal-transducing, heterotrimeric G proteins to determine in vivo interaction of the 2 enzymes, structural analysis
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expression in Escherichia coli; expression of mutant nmt1-181 in Escherichia coli
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expression of His-tagged wild-type and mutants in Escherichia coli
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functional expression in Escherichia coli as His-tagged protein, DNA sequence analysis
gene cloned from cell culture and lymphocytes, in vitro translation of 2 different splice variants, DNA and amino acid sequence determination
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NMT2, DNA and amino acid sequence determination, analysis, and comparisons, phylogenetic tree, expression of His6-tagged NMT2 in Escherichia coli
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overexpression in COS-7 cell, isoform 1 and 2; overexpression in COS-7 cell, isoform 1 and 2
overexpression in COS-7 cell, isoform 1; overexpression in COS-7 cell, isoform 2
recombinant expression of His6-tagged Nef:NMT complex in Escherichia coli Codon Plus (DE-)-RIL cells
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sequence comparisons
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
NMT1 expression in increased in macrophages and neutrophils after Escherichia coli lipopolysacchride application
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A202T
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site-directed mutagenesis, alterations of both peptide and myristoyl binding sites, 3 to 6fold increased Ki for S-(2-oxo)-pentadecyl-CoA and 6 to 9fold increased Ki for SC-58272
C217R
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site-directed mutagenesis, 3 to 6fold increase in Ki for inhibitor SC-58272, selective alteration of the enzymes peptide binding site
D417V
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site-directed mutagenesis, reduced activity, temperature-sensitive
D451K
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site-directed mutagenesis, no functional complementation of enzyme deficient nmt1-181 mutant at 36°C
D451N
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site-directed mutagenesis, no functional complementation of enzyme deficient nmt1-181 mutant at 36°C
E167K
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site-directed mutagenesis, coexpression of wild-type with Asp451, functional complementation of enzyme deficient nmt1-181 mutant at 36°C
E293K
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site-directed mutagenesis, coexpression of wild-type with Asp451, functional complementation of enzyme deficient nmt1-181 mutant at 36°C
F170A/L171A
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site-directed mutagenesis, increased Ki for S-(2-oxo)-pentadecyl-CoA, increased Km for peptide substrate, altered enzyme conformation which modifies myristoyl-CoA polarization during catalytic reaction
F413S
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site-directed mutagenesis, reduced activity, temperature-sensitive
K389I
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site-directed mutagenesis, reduced activity, temperature-sensitive
L171S
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site-directed mutagenesis, reduced activity, temperature-sensitive
L408S
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site-directed mutagenesis, reduced activity, temperature-sensitive
L420S
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site-directed mutagenesis, reduced activity, temperature-sensitive
N102T
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site-directed mutagenesis, reduced activity, temperature-sensitive
N169L
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site-directed mutagenesis, slightly increased Km for peptide substrate, altered kinetics
N169L/T205A
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site-directed mutagenesis, increased Km for peptide substrate, altered kinetics
N426I
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site-directed mutagenesis, mutation of myristoyl-binding site
V395D
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site-directed mutagenesis, reduced activity, temperature-sensitive
additional information
additional information
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transgenic plants expressing the enzyme under control of the cauliflower mosaic virus 35S promotor, down-regulation by anti-sense expression leads to a growth reduced or lethal phenotype
additional information
transgenic plants expressing the enzyme under control of the cauliflower mosaic virus 35S promotor, down-regulation by anti-sense expression leads to a growth reduced or lethal phenotype
additional information
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NMT1 knockdown increases apoptosis in activated neutrophils
additional information
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diverse mutants, evaluation of inhibition mechanism of inhibitor SC-58272 and compounds 1-5
additional information
selectively depletion by siRNA of NMT1 and/or NMT2 from HEK-293T cells expressing a recombinant NefsgGFP fusion protein, NMT1 depletion has minimal effect on the intracellular distribution of Nef-sgGFP, whereas depletion of NMT2 alters distribution to a diffuse, widespread pattern, mimicking that of a myristoylation-deficient mutant of Nef-sgGFP, overview; selectively depletion by siRNA of NMT1 and/or NMT2 from HEK-293T cells expressing a recombinant NefsgGFP fusion protein, NMT1 depletion has minimal effect on the intracellular distribution of Nef-sgGFP, whereas depletion of NMT2 alters distribution to a diffuse, widespread pattern, mimicking that of a myristoylation-deficient mutant of Nef-sgGFP, overview
additional information
selectively depletion by siRNA of NMT1 and/or NMT2 from HEK-293T cells expressing a recombinant NefsgGFP fusion protein, NMT1 depletion has minimal effect on the intracellular distribution of Nef-sgGFP, whereas depletion of NMT2 alters distribution to a diffuse, widespread pattern, mimicking that of a myristoylation-deficient mutant of Nef-sgGFP, overview; selectively depletion by siRNA of NMT1 and/or NMT2 from HEK-293T cells expressing a recombinant NefsgGFP fusion protein, NMT1 depletion has minimal effect on the intracellular distribution of Nef-sgGFP, whereas depletion of NMT2 alters distribution to a diffuse, widespread pattern, mimicking that of a myristoylation-deficient mutant of Nef-sgGFP, overview
additional information
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NMT1 knockout in U-937 cells by siRNA leads to defective monocytic differentiation
additional information
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characterziation of a truncation mutant devoid of 28 N-terminal amino acids from the catalytic module. The deletion of the N-terminal peptide has no effect on the enzyme stability. Mutant displays an 3fold increase in enzymatic. The N-terminal region in the catalytic module serves as a regulatory control element
additional information
enzyme knockout leads to defective myelopoesis, NMT1 knockout in U-937 cells leads to defective monocytic differentiation. Suppressed macrophage colony forming units are observed in M-CSF-stimulated bone marrow cells from heterozygous Nmt1-deficient mice, while homozygous Nmt1-deficient mouse embryonic stem cells show a drastic reduction of macrophages when stimulated to differentiate by M-CSF
additional information
enzyme knockout leads to defective myelopoesis, NMT1 knockout in U-937 cells leads to defective monocytic differentiation. Suppressed macrophage colony forming units are observed in M-CSF-stimulated bone marrow cells from heterozygous Nmt1-deficient mice, while homozygous Nmt1-deficient mouse embryonic stem cells show a drastic reduction of macrophages when stimulated to differentiate by M-CSF
additional information
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temperature sensitive mutant strain nmt1-181, exchange of Gly to Asp, 10fold increased Km for myristoyl-CoA at 36°C
additional information
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disruption or deletion of nmt1-gene causes recessive lethality; temperature sensitive mutant strain nmt1-181, exchange of Gly to Asp, 10fold increased Km for myristoyl-CoA at 36°C
additional information
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C-terminal deletion mutants M454 and L455 produce a 300-400fold reduction in the chemical transformation rate, shift of the rate-limite of the process steps
additional information
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knockdown of NMT expression by tetracycline-inducible RNA interference leads to cell death with a block in endocytosis, but vesicle accumulation around the flagellar pocket indicates a defect in vesicular progression following endocytic fusion. Induced parasites have a wild-type or slightly enlarged Golgi apparatus, phenotype and pleiotropic effects, overview
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
molecular biology
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the enzyme can be used for protein N-myristoylation as a tag labeling technique in recombinant expresssion systems. CaNMT is an effective tool for in vitro and in vivo transfer of an azide-modified acid to the N-terminus of a polypeptide derived from a species entirely unrelated to Candida albicans
synthesis
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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
analysis
the automated assay can be used for proteomic studies to determine the myristoylation state of any protein
analysis
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the automated assay can be used for proteomic studies to determine the myristoylation state of any protein
drug development
the enzyme is a potential target for development of therapeutic agents against visceral leishmaniasis; the enzyme is a potential target for drug development
drug development
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the enzyme is a target for drug design in the treatment of epilepsy
drug development
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the enzyme N-myristoyltransferase represents a promising drug target
medicine
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since myristoylation has a central role in virus maturation and oncogenesis, specific NMT inhibitors might lead to potent antivirus and anticancer agents
medicine
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both NMT1 and hnRNP A2/B1 may take part in the regulation of HIV-1 RNA expression through their mutual opposite effects on the viral RNA expression in HIV-1-producing cells
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.97)
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