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) Rattus norvegicus and UniProt Accession Q8K1Q0

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:
Rattus norvegicus
UNIPROT: Q8K1Q0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Rattus norvegicus
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
-
myristoyl-CoA:protein N-myristoyltransferase 1
-
myristoyltransferase
-
peptide N-myristoyltransferase 1
-
type I N-myristoyltransferase
-
myristoyl-CoA-protein N-myristoyltransferase
-
-
-
-
myristoyl-CoA: protein N-myristoyltransferase
-
myristoyl-CoA:protein N-myristoyltransferase
-
-
myristoyl-coenzyme A:protein N-myristoyl transferase
-
-
-
-
myristoylating enzymes
-
-
-
-
myristoyltransferase, protein N-
-
-
-
-
N-myristoyltransferase
-
-
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 + GAQLSTLSRV
myristoylglycyl-AQLSTLSRV + CoA
show the reaction diagram
-
-
-
?
lauroyl-CoA + glycylpeptide
N-lauroylglycylpeptide + CoA
show the reaction diagram
-
-
-
-
?
myristoleoyl-CoA + glycylpeptide
N-myristoleoylglycylpeptide + CoA
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + cAMP-dependent protein kinase-derived peptide
N-myristoylated cAMP-dependent protein kinase-derived peptide + CoA
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + GAQLSTLSRV
myristoylglycyl-AQLSTLSRV + CoA
show the reaction diagram
-
-
-
?
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 + glycylpeptide
N-myristoylglycylpeptide + CoA
show the reaction diagram
myristoyl-CoA + p60src-derived peptide
N-myristoylated p60src-derived peptide + CoA
show the reaction diagram
n-decanoyl-CoA + glycylpeptide
N-decanoylglycylpeptide + CoA
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
show the reaction diagram
-
no activity
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
show the reaction diagram
-
-
-
-
?
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoylglycylpeptide
show the reaction diagram
additional information
?
-
-
the enzyme catalyzes the cotranslational irreversible addition of a fatty acyl moiety to 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
tetradecanoyl-CoA + glycylpeptide
CoA + N-tetradecanoyl-glycylpeptide
show the reaction diagram
-
-
-
-
?
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
?
-
-
the enzyme catalyzes the cotranslational irreversible addition of a fatty acyl moiety to the N-terminus of proteins
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
enolase
-
-
-
N-Myristoylglycylpeptides
-
-
-
palmitoyl-CoA
-
-
protein NIP71
-
protein from bovine brain
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxycholate
-
2% w/v, activation by pretreatment
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.117
cAMP-dependent protein kinase-derived peptide
-
0.02 - 0.06
p60src-derived peptide
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000019
-
microsomes from brain
0.0000029
-
-
0.00076
-
partially purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NMT1_RAT
496
0
56860
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
-
1 * 48000, splice variant 2, SDS-PAGE
55000
additional information
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
expression in COS-7 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lipopolysaccharides increase the enzyme expression in lungs
-
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
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
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
McIlhinney, R.A.J.; McGlone, K.
Characterisation of a myristoyl CoA:glycylpeptide N-myristoyl transferase activity in rat brain: subcellular and regional distribution
J. Neurochem.
54
110-117
1990
Rattus norvegicus
Manually annotated by BRENDA team
McIlhinney, R.A.J.; McGlone, K.
Characterization, regional and subcellular distribution of an N-myristoyl-CoA:glycyltransferase activity in rat brain
Biochem. Soc. Trans.
17
888-889
1989
Rattus norvegicus
-
Manually annotated by BRENDA team
Glover, C.J.; Goddard, C.; Felsted, R.L.
N-myristoylation of p60src. Identification of a myristoyl-CoA:glycylpeptide N-myristoyltransferase in rat tissues
Biochem. J.
250
485-491
1988
Rattus norvegicus
Manually annotated by BRENDA team
Towler, D.A.; Adams, S.P.; Eubanks, S.R.; Towery, D.S.; Jackson-Machelski, E.; Glaser, L.; Gordon, J.I.
Myristoyl CoA: protein N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities
J. Biol. Chem.
263
1784-1790
1988
Rattus norvegicus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Raju, R.V.S.; Datla, R.S.S.; Warrington, R.C.; Sharma, R.K.
Effects of L-histidine and its structural analogs on human N-myristoyltransferase activity and importance of EEVEH amino acid sequence for enzyme activity
Biochemistry
37
14928-14936
1998
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
McIlhinney, R.A.; Young, K.; Egerton, M.; Camble, R.; White, A.; Soloviev, M.
Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme
Biochem. J.
333
491-495
1998
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Shrivastav, A.; Selvakumar, P.; Bajaj, G.; Lu, Y.; Dimmock, J.R.; Sharma, R.K.
Regulation of N-myristoyltransferase by novel inhibitor proteins
Cell Biochem. Biophys.
43
189-202
2005
Rattus norvegicus
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
Pasha, M.K.; Sharma, R.K.; Rajput, A.H.
Increased myocardial N-myristoyltransferase activity in rotenone model of Parkinsonism
Int. J. Mol. Med.
15
987-991
2005
Rattus norvegicus
Manually annotated by BRENDA team
Rioux, V.; Beauchamp, E.; Pedrono, F.; Daval, S.; Molle, D.; Catheline, D.; Legrand, P.
Identification and characterization of recombinant and native rat myristoyl-CoA: protein N-myristoyltransferases
Mol. Cell. Biochem.
286
161-170
2006
Rattus norvegicus (Q700Q7), Rattus norvegicus (Q8K1Q0)
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
Charavaryamath, C.; Lemieux, H.; Singh Suri, S.; Selvakumar, P.; Sharma, R.K.; Singh, B.
Expression and activities of N-myristoyltransferase and calcineurin in normal and inflamed lungs
Exp. Lung Res.
35
729-747
2009
Rattus norvegicus
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