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Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase and Organism(s) Bos taurus and UniProt Accession P31717

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IUBMB Comments
The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
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Bos taurus
UNIPROT: P31717
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The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Synonyms
n-myristoyltransferase, nmt-1, myristoyl-coa:protein n-myristoyltransferase, n-myristoyl transferase, nmt1p, n-myristoyltransferase 1, myristoyltransferase, canmt, myristoyl-coa protein n-myristoyltransferase, tbnmt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycylpeptide N-tetradecanoyltransferase 1
-
myristoyl-CoA:protein N-myristoyltransferase 1
-
myristoyltransferase
-
peptide N-myristoyltransferase 1
-
type I N-myristoyltransferase
-
dipeptide N-myristoyltransferase 2
-
glycylpeptide N-tetradecanoyltransferase 2
-
myristoyl-CoA-protein N-myristoyltransferase
-
-
-
-
myristoyl-CoA:protein N-myristoyltransferase
-
-
myristoyl-CoA:protein N-myristoyltransferase 2
-
myristoyl-CoA:protein N-myristoyltransferase type 2
-
myristoyl-coenzyme A:protein N-myristoyl transferase
-
-
-
-
myristoylating enzymes
-
-
-
-
myristoyltransferase
-
myristoyltransferase, protein N-
-
-
-
-
N-myristoyltransferase
-
-
peptide N-myristoyltransferase
-
-
-
-
protein N-myristoyltransferase
-
-
-
-
type II N-myristoyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
show the reaction diagram
PEST regions for recognition by clapains, putative regulatory enzymes
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
Acyl group transfer
-
-
-
-
amide bond formation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
tetradecanoyl-CoA:N-terminal-glycine-[protein] N-tetradecanoyltransferase
The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
CAS REGISTRY NUMBER
COMMENTARY hide
110071-61-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
show the reaction diagram
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys-Arg + CoA
show the reaction diagram
-
pp60src-derived peptide
-
-
?
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
show the reaction diagram
-
pp60src-derived peptide
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
myristoyl-CoA + M2 gene segment of reovirus type 3-derived peptide
N-myristoylated M2 gene segment of reovirus type 3-derived peptide + CoA
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
show the reaction diagram
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
show the reaction diagram
-
poor substrate
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
show the reaction diagram
-
i.e. myristoyl-CoA, the enzyme attaches the fatty acid to a glycine at the N-terminus of proteins
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
-
enzyme is possibly regulated by calpains in vivo
-
-
?
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
show the reaction diagram
-
retina enzyme
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
show the reaction diagram
-
i.e. myristoyl-CoA, the enzyme attaches the fatty acid to a glycine at the N-terminus of proteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
40% inhibition at 5 mM, activation at lower concentrations below 0.25 mM
factor NIP71
-
competitive against activation factor NAF45
-
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
-
Mn2+
50% inhibition at 5 mM
Zn2+
80% inhibition at 5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-myristoyltransferase activator NAF45
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.2
cAMP-dependent protein kinase-derived peptide
-
0.05
M2 gene segment of reovirus type 3-derived peptide
-
recombinant enzyme
-
0.0058
myristoyl-CoA
-
recombinant enzyme
0.016 - 0.04
p60src-derived peptide
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.048
-
purified recombinant protein
0.096
-
partially puified enzyme
0.1
-
purified enzyme
additional information
-
activity of purified inhibitor protein from brain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cardiac, low activity
Manually annotated by BRENDA team
-
elevated NMT1 expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
lung, NMT1
Manually annotated by BRENDA team
-
airway, NMT1
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
intravascular, high NMT1 expression
Manually annotated by BRENDA team
-
high NMT1 expression in neutrophils from the necrotic areas in inflamed lungs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
NMT1 in endothelium
Manually annotated by BRENDA team
-
occasionally
Manually annotated by BRENDA team
-
occasionally
Manually annotated by BRENDA team
-
NMT1 in endothelium
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
expression of isozyme NMT1 is reduced in lung inflammation and induced by Mannheimer hemolytica, probably due to increased enolase expression
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NMT1_BOVIN
497
0
56919
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
126000 - 390000
-
high molecular weight aggregates, gel filtration
43000
-
1 * 43000, active low MW form generated by proteolysis during storage, SDS-PAGE
50000
55000
-
gel filtration
60000
60000 - 66000
-
gel filtration, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, recombinant His6-tagged brain NMT2, SDS-PAGE
monomer
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
NMT1 knockdown increases apoptosis in activated neutrophils
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, conversion of 60000 Da form into 47000 Da form, loss of 30% activity within 10 days
-
4°C, conversion of 60000 Da form into 47000 Da form, activity is stable over several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cardiac muscle enzyme, recombinant from Escherichia coli
-
isoform from brain bound to NAF45
-
multiple forms from brain
-
partial
-
recombinant His6-tagged NMT2 from Escherichia coli by nickel affinity chromatography to homogeneity
spleen enzyme, recombinant from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of cardiac muscle enzyme, expression in Escherichia coli, DNA and amino acid sequence determination
-
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
-
NMT2, DNA and amino acid sequence determination, analysis, and comparisons, phylogenetic tree, expression of His6-tagged NMT2 in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
NMT1 expression in increased in macrophages and neutrophils after Escherichia coli lipopolysacchride application
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of activity by rebuilding enzyme-NAF45 complex
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
King, M.J.; Sharma, R.K.
Identification, purification and characterization of a membrane-associated N-myristoyltransferase inhibitor protein from bovine brain
Biochem. J.
291
635-639
1993
Bos taurus
Manually annotated by BRENDA team
McIlhinney, R.A.J.; McGlone, K.; Willis, A.C.
Purification and partial sequencing of myristoyl-CoA:protein N-myristoyltransferase from bovine brain
Biochem. J.
290
405-410
1993
Bos taurus
-
Manually annotated by BRENDA team
McIlhenney, R.A.J.; McGlone, K.
Characterization of the myristoyl CoA:glycylpeptide N-myristoyl transferase from rat and bovine brain
Biochem. Soc. Trans.
20
341S
1992
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
King, M.J.; Sharma, R.K.
Differential activation of bovine brain N-myristoyltransferase(s) by a cytosolic activator
Biochem. Biophys. Res. Commun.
212
580-588
1995
Bos taurus
Manually annotated by BRENDA team
Glover, C.J.; Felsted, R.L.
Identification and characterization of multiple forms of bovine brain N-myristoyltransferase
J. Biol. Chem.
270
23226-23233
1995
Bos taurus
Manually annotated by BRENDA team
Raju, R.V.S.; Datla, R.S.S.; Kakkarl, R.; Sharma, R.K.
Recombinant bovine spleen myristoyl CoA: protein N-myristoyltransferase
Mol. Cell. Biochem.
189
91-97
1998
Bos taurus
Manually annotated by BRENDA team
Raju, R.V.S.; Kakkar, R.; Datla, R.S.S.; Radhi, J.; Sharma, R.K.
Myristoyl-CoA:protein N-myristoyltransferase from bovine cardiac muscle: molecular cloning, kinetic analysis, and in vitro proteolytic cleavage by m-calpain
Exp. Cell Res.
241
23-35
1998
Bos taurus
Manually annotated by BRENDA team
Rundle, D.R.; Rajala, R.V.; Anderson, R.E.
Characterization of Type I and Type II myristoyl-CoA:protein N-myristoyltransferases with the Acyl-CoAs found on heterogeneously acylated retinal proteins
Exp. Eye Res.
75
87-97
2002
Bos taurus
Manually annotated by BRENDA team
Shrivastav, A.; Pasha, M.K.; Selvakumar, P.; Singh, B.; Sharma, R.K.
Expression, localization, and correlation of N-myristoyltransferase and its inhibitor in bovine eye
Invest. Ophthalmol. Vis. Sci.
45
1674-1679
2004
Bos taurus
Manually annotated by BRENDA team
Rundle, D.R.; Rajala, R.V.; Alvarez, R.A.; Anderson, R.E.
Myristoyl-CoA:protein N-myristoyltransferases: isoform identification and gene expression in retina
Mol. Vis.
10
177-185
2004
Bos taurus
Manually annotated by BRENDA team
Selvakumar, P.; Lakshmikuttyamma, A.; Charavaryamath, C.; Singh, B.; Tuchek, J.; Sharma, R.K.
Expression of myristoyltransferase and its interacting proteins in epilepsy
Biochem. Biophys. Res. Commun.
335
1132-1139
2005
Bos taurus, Saccharomyces cerevisiae, Candida sp. (in: Saccharomycetales), Oryctolagus cuniculus, Dictyostelium sp., Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Selvakumar, P.; Lakshmikuttyamma, A.; Shrivastav, A.; Das, S.B.; Dimmock, J.R.; Sharma, R.K.
Potential role of N-myristoyltransferase in cancer
Prog. Lipid Res.
46
1-36
2007
Oryctolagus cuniculus, Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens, Saccharomyces cerevisiae (P14743), Bos taurus (P31717), Bos taurus (Q9N181), Rattus norvegicus (Q8K1Q0)
Manually annotated by BRENDA team
Selvakumar, P.; Lakshmikuttyamma, A.; Sharma, R.K.
Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2
J. Biomed. Biotechnol.
2009
907614
2009
Bos taurus (Q9N181), Bos taurus
Manually annotated by BRENDA team
Shrivastav, A.; Suri, S.; Mohr, R.; Janardhan, K.; Sharma, R.; Singh, B.
Expression and activity of N-myristoyltransferase in lung inflammation of cattle and its role in neutrophil apoptosis
Vet. Res.
41
9
2010
Bos taurus
Manually annotated by BRENDA team