Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase and Organism(s) Mus musculus and UniProt Accession O70310

for references in articles please use BRENDA:EC2.3.1.97
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: O70310
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
N-myristoyltransferase 1
-
myristoyl-CoA-protein N-myristoyltransferase
-
-
-
-
myristoyl-coenzyme A:protein N-myristoyl transferase
-
-
-
-
myristoylating enzymes
-
-
-
-
myristoyltransferase, protein N-
-
-
-
-
N-myristoyltransferase
-
-
N-myristoyltransferase 1
-
-
NMT1
-
-
peptide N-myristoyltransferase
-
-
-
-
protein 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
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
-
-
-
?
tetradecanoyl-CoA + glycyl-pp60cSrc
CoA + N-tetradecanoyl-glycyl-pp60cSrc
show the reaction diagram
i.e. myristoyl-CoA
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
show the reaction diagram
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Arg-Arg + CoA
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + Gly-Gln-Thr-Val-Thr-Thr-Pro-Leu
N-myristoyl-Gly-Gln-Thr-Val-Thr-Thr-Pro-Leu + CoA
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
tetradecanoyl-CoA + glycyl-pp60c Src
CoA + N-tetradecanoyl-glycyl-pp60c Src
show the reaction diagram
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tetradecanoyl-CoA + glycyl-pp60cSrc
CoA + N-tetradecanoyl-glycyl-pp60cSrc
show the reaction diagram
i.e. myristoyl-CoA
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
tetradecanoyl-CoA + glycyl-pp60c Src
CoA + N-tetradecanoyl-glycyl-pp60c Src
show the reaction diagram
i.e. myristoyl-CoA
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
show the reaction diagram
-
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
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heat shock cognate protein 70
involved in NMT1 regulation, overview
-
1-Bromo-2-fluorotetradecane
-
-
1-O-Acetyl-2-fluorotetradecane
-
-
2-Bromomyristic acid
-
-
2-bromomyristoyl-CoA
-
-
2-Fluoromyristic acid
-
-
2-fluoromyristoyl-CoA
-
-
2-Fluorotetradecan-1-ol
-
-
2-Hydroxymyristic acid
-
-
2-hydroxymyristoyl-CoA
-
-
heat shock cognate protein 70
involved in NMT1 regulation, overview
-
S-(2-Oxo)-pentadecyl-CoA
-
strong
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
-
2% w/v, activation by pretreatment
Triton 770
-
2% w/v, activation by pretreatment
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33
Gly-Asn-Ala-Ala-Ala-Arg-Arg
-
-
0.17
Gly-Gln-Thr-Val-Thr-Thr-Pro-Leu
-
-
0.033
Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro
-
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
2-Bromomyristic acid
-
-
0.45
2-bromomyristoyl-CoA
-
-
0.2
2-fluoromyristoyl-CoA
-
-
0.2
2-Hydroxymyristic acid
-
-
0.045
2-hydroxymyristoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000021
-
microsomes from leukemia cell line L1210
0.0000076
-
microsomes from liver
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
leukemic cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
predominantly
Manually annotated by BRENDA team
-
enzyme interacts with calnexin at the endoplasmic reticulum
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme knockout leads to defective myelopoesis
physiological function
NMT1 is required in the development of monocytic lineage and essential for the early development of mouse embryo
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
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NMT1_MOUSE
496
0
56888
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-100°C, 20 mM Tris/HCl buffer, pH 7.1, 1 mM EDTA, 1 mM DTT, 25% glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in COS-7 cell, isoform 1
overexpression in COS-7 cell, isoform 2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Towler, D.A.; Gordon, J.I.; Adams, S.P.; Glaser, L.
The biology and enzymology of eukaryotic protein acylation
Annu. Rev. Biochem.
57
69-99
1988
Saccharomyces cerevisiae, Mus musculus, Rattus norvegicus, Triticum aestivum
Manually annotated by BRENDA team
Boutin, J.A.; Clarenc, J.P.; Ferry, G.; Ernould, A.P.; Remond, G.; Vincent, M.; Atassi, G.
N-myristoyl-transferase activity in cancer cells. Solubilization, specificity and enzymatic inhibition of a N-myristoyl transferase from L1210 microsomes
Eur. J. Biochem.
201
257-263
1991
Saccharomyces cerevisiae, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Paige, L.A.; Zheng, G.Q.; DeFrees, S.A.; Cassady, J.M.; Geahlen, R.L.
Metabolic activation of 2-substituted derivatives of myristic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase
Biochemistry
29
10566-10573
1990
Mus musculus
Manually annotated by BRENDA team
Paige, L.A.; Chafin, D.R.; Cassady, J.M.; Geahlen, R.L.
Detection of myristoyl CoA:protein N-myristoyltransferase activity by ion-exchange chromatography
Anal. Biochem.
181
254-258
1989
Mus musculus
Manually annotated by BRENDA team
Towler, D.A.; Eubanks, S.R.; Towery, D.S.; Adams, S.P.; Glaser, L.
Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase
J. Biol. Chem.
262
1030-1036
1987
Saccharomyces cerevisiae, Mus musculus
Manually annotated by BRENDA team
Giang, D.K.; Cravatt, B.F.
A second mammalian N-myristoyltransferase
J. Biol. Chem.
273
6595-6598
1998
Homo sapiens (O60551), Homo sapiens (P30419), Homo sapiens, Mus musculus (O70310), Mus musculus (O70311), Mus musculus
Manually annotated by BRENDA team
Yang, S.H.; Shrivastav, A.; Kosinski, C.; Sharma, R.K.; Chen, M.H.; Berthiaume, L.G.; Peters, L.L.; Chuang, P.T.; Young, S.G.; Bergo, M.O.
N-myristoyltransferase 1 is essential in early mouse development
J. Biol. Chem.
280
18990-18995
2005
Mus musculus
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
Shrivastav, A.; Varma, S.; Lawman, Z.; Yang, S.H.; Ritchie, S.A.; Bonham, K.; Singh, S.M.; Saxena, A.; Sharma, R.K.
Requirement of N-myristoyltransferase 1 in the development of monocytic lineage
J. Immunol.
180
1019-1028
2008
Homo sapiens, Mus musculus (O70310), Mus musculus (O70311), Mus musculus
Manually annotated by BRENDA team
Kumar, S.; Singh, B.; Dimmock, J.R.; Sharma, R.K.
N-myristoyltransferase in the leukocytic development processes
Cell Tissue Res.
345
203-211
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Dudek, E.; Millott, R.; Liu, W.X.; Beauchamp, E.; Berthiaume, L.G.; Michalak, M.
N-myristoyltransferase 1 interacts with calnexin at the endoplasmic reticulum
Biochem. Biophys. Res. Commun.
468
889-893
2015
Mus musculus
Manually annotated by BRENDA team