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Literature summary for 2.3.1.97 extracted from

  • Kumar, S.; Singh, B.; Dimmock, J.R.; Sharma, R.K.
    N-myristoyltransferase in the leukocytic development processes (2011), Cell Tissue Res., 345, 203-211.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
tetradecanoyl-CoA + glycylpeptide Mus musculus 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 CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide Homo sapiens 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 CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide Rattus norvegicus 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 CoA + N-tetradecanoylglycylpeptide
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isozymes NMT1 and NMT2
-
Mus musculus
-
isozymes NMT1 and NMT2
-
Rattus norvegicus
-
isozymes NMT1 and NMT2
-

Reaction

Reaction Comment Organism Reaction ID
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] 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 Mus musculus
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] 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 Homo sapiens
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] 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 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
bone marrow cell
-
Homo sapiens
-
bone marrow cell 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 Mus musculus
-
bone marrow cell 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 Rattus norvegicus
-
colon 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 Homo sapiens
-
colonic cancer cell
-
Rattus norvegicus
-
colonic neoplasm cell 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 Homo sapiens
-
leukocyte
-
Mus musculus
-
leukocyte
-
Homo sapiens
-
leukocyte
-
Rattus norvegicus
-
macrophage
-
Mus musculus
-
macrophage
-
Homo sapiens
-
macrophage
-
Rattus norvegicus
-
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 Rattus norvegicus
-
neutrophil
-
Mus musculus
-
neutrophil
-
Homo sapiens
-
neutrophil
-
Rattus norvegicus
-
peripheral blood mononuclear cell
-
Mus musculus
-
peripheral blood mononuclear cell
-
Homo sapiens
-
peripheral blood mononuclear cell 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 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tetradecanoyl-CoA + glycylpeptide
-
Mus musculus CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide
-
Homo sapiens CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide
-
Rattus norvegicus CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide 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 Mus musculus CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide 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 Homo sapiens CoA + N-tetradecanoylglycylpeptide
-
?
tetradecanoyl-CoA + glycylpeptide 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 Rattus norvegicus CoA + N-tetradecanoylglycylpeptide
-
?

Subunits

Subunits Comment Organism
More 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 Mus musculus
More 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 Homo sapiens
More 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 Rattus norvegicus

Synonyms

Synonyms Comment Organism
N-myristoyltransferase
-
Mus musculus
N-myristoyltransferase
-
Homo sapiens
N-myristoyltransferase
-
Rattus norvegicus
NMT
-
Mus musculus
NMT
-
Homo sapiens
NMT
-
Rattus norvegicus
NMT1
-
Mus musculus
NMT1
-
Homo sapiens
NMT1
-
Rattus norvegicus
NMT2
-
Mus musculus
NMT2
-
Homo sapiens
NMT2
-
Rattus norvegicus

General Information

General Information Comment Organism
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 Mus musculus
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 Homo sapiens
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 Rattus norvegicus
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 Mus musculus
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 Mus musculus
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 Homo sapiens
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 Rattus norvegicus