2.3.1.97: glycylpeptide N-tetradecanoyltransferase
This is an abbreviated version!
For detailed information about glycylpeptide N-tetradecanoyltransferase, go to the full flat file.
Word Map on EC 2.3.1.97
-
2.3.1.97
-
myristate
-
n-myristoylation
-
albicans
-
leishmania
-
octapeptide
-
co-translational
-
pp60src
-
14-carbon
-
nonmyristoylated
-
medicine
-
benzofuran
-
drug development
-
molecular biology
-
synthesis
-
analysis
- 2.3.1.97
- myristate
-
n-myristoylation
- albicans
- leishmania
- octapeptide
-
co-translational
-
pp60src
-
14-carbon
-
nonmyristoylated
- medicine
- benzofuran
- drug development
- molecular biology
- synthesis
- analysis
Reaction
Synonyms
CaNMT, cell division control protein 72, dipeptide N-myristoyltransferase 2, glycylpeptide N-tetradecanoyltransferase, glycylpeptide N-tetradecanoyltransferase 1, glycylpeptide N-tetradecanoyltransferase 2, HsNMT1, HsNMT2, LmNMT, More, myristoyl-CoA-protein N-myristoyltransferase, myristoyl-CoA: protein N-myristoyltransferase, myristoyl-CoA:protein N-myristoyltransferase, myristoyl-CoA:protein N-myristoyltransferase 1, myristoyl-CoA:protein N-myristoyltransferase 2, myristoyl-CoA:protein N-myristoyltransferase type 2, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoyl-coenzyme A:protein N-myristoyltransferase, myristoylating enzymes, myristoyltransferase, myristoyltransferase type 1, myristoyltransferase, protein N-, N-myristoyl transferase, N-myristoyltransferase, N-myristoyltransferase 1, N-myristoyltransferase 2, NMT, NMT 1, NMT 2, NMT-1, NMT-2, NMT1, Nmt1p, NMT2, peptide N-myristoyltransferase, peptide N-myristoyltransferase 1, peptide N-myristoyltransferase 2, protein N-myristoyltransferase, PVX_085815, TbNMT, type I N-myristoyltransferase, type II N-myristoyltransferase
ECTree
2.3.1.97 glycylpeptide N-tetradecanoyltransferaseAdvanced search results
results (
results (General Information
General Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
-
both N-myristoyltransferases NMT1 and NMT2 are cleaved during apoptosis. The caspase-3- or -8-mediated cleavage of NMT1 at Asp72 precedes the cleavage of NMT2 by caspase-3 mainly at Asp25. The cleavage of NMTs does not significantly affect their activity in apoptotic cells until the 8 h time point. The cleavage of the predominantly membrane bound NMT1 removes a polybasic domain stretch and leads to a cytosolic relocalization, whereas predominantly cytosolic NMT2 relocalizes to membranes when cleaved after the removal of a negatively charged domain
physiological function
additional information
-
human NMT-1 specifically myristoylates Nef and the two proteins are able to remain associated through immunoprecipitation and purification steps, Nef:NMT complex structure analysis, overview
evolution
-
N-myristoyltransferase is an ubiquitously distributed enzyme and belongs to the GCN5 acetyltransferase superfamily. NMT exists as a single copy gene in lower eukaryotes, whereas in higher eukaryotes, two genes encoding for the two isoforms of NMT have been identified. The NMT1 isoform is homologous to the NMT from lower eukaryotes
evolution
-
N-myristoyltransferase is an ubiquitously distributed enzyme and belongs to the GCN5 acetyltransferase superfamily. NMT exists as a single copy gene in lower eukaryotes, whereas in higher eukaryotes, two genes encoding for the two isoforms of NMT have been identified. The NMT1 isoform is homologous to the NMT from lower eukaryotes
evolution
-
N-myristoyltransferase is an ubiquitously distributed enzyme and belongs to the GCN5 acetyltransferase superfamily. NMT exists as a single copy gene in lower eukaryotes, whereas in higher eukaryotes, two genes encoding for the two isoforms of NMT have been identified. The NMT1 isoform is homologous to the NMT from lower eukaryotes
malfunction
-
expression of isozyme NMT1 is reduced in lung inflammation and induced by Mannheimer hemolytica, probably due to increased enolase expression
malfunction
-
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
-
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
NMT function is essential for viability in host cells and in insect stages of the pathogenic protozoan parasite
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
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
physiological function
-
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
-
expression of NMT gene is essential for survival of Trypanosoma cruzi epimastigotes
physiological function
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
-
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
-
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
acyl-CoA binding protein, acyl-CoA binding domain (ACBD)6, stimulates the myristoyltransferase reaction of isoform NMT2. The stimulatory effect requires interaction between ACBD6 and NMT2, and is enhanced by binding of ACBD6 to its ligand, C18:2 -CoA. The presence of ACBD6 prevents competition of the myristoyltransferase reaction by C16 -CoA. Mutants of ACBD6 that are either deficient in ligand binding to the N-terminal ACBD or unable to interact with NMT2 do not stimulate activity of NMT2, nor can they protect the enzyme from utilizing the competitor C16 -CoA
physiological function
-
expression in Escherichia coli mutant having lipid A containing only 3-hydroxymyristic acids, leads to lipid A with two additional myristic acids (C14:0). When the gene is introduced into a mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0. C12:0 in lipid A can be replaced by C14:0 without changing the immunostimulating activity
physiological function
Klebsiella pneumoniae NBRC 14940T
-
expression in Escherichia coli mutant having lipid A containing only 3-hydroxymyristic acids, leads to lipid A with two additional myristic acids (C14:0). When the gene is introduced into a mutant with pentaacylated lipid A containing one lauric acid (C12:0), C12:0 is replaced by C14:0. C12:0 in lipid A can be replaced by C14:0 without changing the immunostimulating activity
-
physiological function
-
NMT function is essential for viability in host cells and in insect stages of the pathogenic protozoan parasite
-
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
-
physiological function
-
expression of the Nmt gene is essential for viability. Partial repression of the gene reveals downstream effects of N-myristoylation on cell wall morphology
-
