Any feedback?
Information on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P14743
for references in articles please use BRENDA:EC2.3.1.97Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.97 glycylpeptide N-tetradecanoyltransferaseIUBMB 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
Word Map
- 2.3.1.97
- myristate
-
n-myristoylation
- albicans
- leishmania
- octapeptide
-
co-translational
-
pp60src
-
14-carbon
-
nonmyristoylated
- medicine
- benzofuran
- drug development
- molecular biology
- synthesis
- analysis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
myristoyl-CoA-protein N-myristoyltransferase
-
-
-
-
myristoyl-coenzyme A:protein N-myristoyl transferase
-
-
-
-
myristoylating enzymes
-
-
-
-
myristoyltransferase, protein N-
-
-
-
-
NMT
-
-
peptide N-myristoyltransferase
-
-
-
-
protein N-myristoyltransferase
-
-
-
-
additional information
additional information
enzyme belongs to the superfamily of GCN5-related N-acetyltransferases
additional information
-
enzyme belongs to the superfamily of GCN5-related N-acetyltransferases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
ordered bi bi mechanism
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
detailed mechanism
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
kinetic analysis
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
peptide binding site
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
active site
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoyl-CoA binding site
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
mechanism
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
ordered mechanism
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
ordered bi bi mechanism
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
kinetic analysis
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
interactions between enzyme and acyl-CoA and peptide substrates, formation of a high affinity reaction intermediate
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
peptide binding site
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoyl-CoA binding site
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
requires alanine at position 5 of substrate peptides
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
cooperativity between acyl-CoA and peptide binding sites
-
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
110071-61-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
11-oxatetradecanoyl-CoA + G0alpha-hexapeptide
N-11-oxatetradecanoyl-G0alpha-hexapeptide + CoA
-
-
-
-
?
11-phenylundecanoyl-CoA + glycylpeptide
11-phenylundecanoyl-glycylpeptide + CoA
-
-
-
-
?
13-oxatetradecanoyl-CoA + G0alpha-hexapeptide
N-13-oxatetradecanoyl-G0alpha-hexapeptide + CoA
-
-
-
-
?
6-oxatetradecanoyl-CoA + G0alpha-hexapeptide
N-6-oxatetradecanoyl-G0alpha-hexapeptide + CoA
-
-
-
-
?
dodecanoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-dodecanoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val
N-myristoyl-Gly-Ala-Ala-Pro-Ser-Lys-Ile-Val + CoA
-
-
-
?
myristoyl-CoA + Gly-Ala-Arg-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Ala-Arg-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
myristoyl-CoA + Gly-Asn-Ala-Pro-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Pro-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Asn-Phe-Ala-Ala-Ala-Arg-Arg
N-myristoyl-Gly-Asn-Phe-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + Gly-L-Ala-L-Arg-L-Ala-L-Ser-L-Val-L-Leu-L-Ser
N-myristoyl-Gly-L-Ala-L-Arg-L-Ala-L-Ser-L-Val-L-Leu-L-Ser + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Leu-Tyr-Ala-Ser-Lys-Leu-Ser
N-myristoyl-Gly-Leu-Tyr-Ala-Ser-Lys-Leu-Ser + CoA
-
-
-
-
?
myristoyl-CoA + Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys
N-myristoyl-Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys + CoA
-
-
-
-
?
myristoyl-CoA + Pr55gag-precursor-derived octapeptide
N-myristoylated Pr55gag-precursor-derived peptide + CoA
-
peptide substrate is derived from human immunodeficiency virus
-
?
palmitoyl-CoA + Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg
N-palmitoyl-Gly-Asn-Ala-Ala-Ala-Ala-Arg-Arg + CoA
-
-
-
-
?
tetradecanoyl-CoA + GLYASKLA
CoA + N-tetradecanoyl-GLYASKLA
-
i.e. myristoyl-CoA
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
-
-
-
?
myristoyl-CoA + Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg
N-myristoyl-Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
substrate specificity
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by CoA-derivatives of hydroxytetradecanoic acids, azidoaromatic analogues of myristic acid, omega-nitrocarboxylic acids, halogen- and haloaromatic analogues of myristic acid and, with low activity, by dicarboxylic fatty acids
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
stereochemical requirements
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
stereochemical requirements
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
biotinylated peptides
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
altered fatty acid chain length
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-peptides can compete with myristoyl-CoA for the binding site
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by oxygen or sulfur mono-substituted analogs
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by phenyl-, furyl-, thienyl-, acylohexyl-substituted fatty acids
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by unsaturated fatty acids
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
myristoyl-CoA can be replaced by oxygen or sulfur di-substituted analogs
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for uncharged amino acid at position 2 of peptide chain, no peptides with bulky hydrophobic side chains at position 2, broad spectrum of amino acids in position 3, overview
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
overview peptides and proteins
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for Gly at N-terminus
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for myristoyl-CoA
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
specific for myristoyl-CoA
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
p60src-derived peptides
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
p60src-derived peptides
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + protein
?
-
proteins involved in metabolic regulation, e.g. catalytic subunit of protein kinase A and G protein alpha subunit
-
-
?
myristoyl-CoA + protein
?
-
natural protein substrates are: catalytic subunit of cAMP-dependent protein kinase, p60src, phosphatases, e.g. calcineurin B, transmembrane signalling proteins, e.g. alpha-subunits of heterotrimeric G proteins, gag polyprotein precursors of several retroviruses, capsid proteins of some parvoviruses and picornaviruses
-
-
ir
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
-
-
-
?
palmitoyl-CoA + glycylpeptide
N-palmitoylglycylpeptide + CoA
-
poor substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
-
-
ir
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + glycylpeptide
N-myristoylglycylpeptide + CoA
-
enzyme is essential for vegetative growth
-
?
myristoyl-CoA + protein
?
-
proteins involved in metabolic regulation, e.g. catalytic subunit of protein kinase A and G protein alpha subunit
-
-
?
myristoyl-CoA + protein
?
-
natural protein substrates are: catalytic subunit of cAMP-dependent protein kinase, p60src, phosphatases, e.g. calcineurin B, transmembrane signalling proteins, e.g. alpha-subunits of heterotrimeric G proteins, gag polyprotein precursors of several retroviruses, capsid proteins of some parvoviruses and picornaviruses
-
-
ir
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3S)-N-[2-[(cyclopentylcarbonyl)amino]-1,3-benzothiazol-6-yl]-3-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
(4S,5aS,12aS)-2-carbamoyl-4-(dimethylamino)-3,10,12,12a-tetrahydroxy-6-methylidene-1,11-dioxo-1,4,4a,5,5a,6,11,12a-octahydrotetracen-5-yl acetate
-
-
2-(diethylamino)ethyl 2-[(cyclohexylcarbonyl)amino]-1,3-benzothiazole-6-carboxylate
-
-
2-([[4-(aminomethyl)cyclohexyl]carbonyl]amino)-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1-benzofuran-6-ylmethyl)amino]cyclohexyl]carbonyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
2-[([(1R,3S)-3-[(1H-indol-6-ylmethyl)amino]cyclohexyl]acetyl)amino]-N,N-dimethyl-1,3-benzothiazole-6-carboxamide
-
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-ylidene)methanediyl]bis(6-hydroxybenzoic acid)
-
-
3-([3-methyl-2-[(2,3,4-trifluorophenoxy)methyl]-1-benzofuran-4-yl]oxy)-N-(pyridin-3-ylmethyl)propan-1-amine
-
-
4-(4,5-dihydroxy-9-methyl-3-oxo-1,3,3a,4,9,9a-hexahydronaphtho[2,3-c]furan-1-yl)-2,5,6-trihydroxycyclohexa-2,4-diene-1-carboxamide
-
-
Ala-Leu-Tyr-Ala-Ser-Lys-Leu-Ser
-
competitve against peptide substrate Gly-Leu-Tyr-Ala-Ser-Lys-Leu-Ser
cis-4-[(naphthalen-2-ylmethyl)amino]-N-(6-pyridin-2-yl-1,3-benzothiazol-2-yl)cyclohexanecarboxamide
-
-
cis-N-(6-fluoro-1,3-benzothiazol-2-yl)-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
cis-N-1,3-benzothiazol-2-yl-4-[(naphthalen-2-ylmethyl)amino]cyclohexanecarboxamide
-
-
ethyl 3-methyl-4-[3-[(pyridin-3-ylmethyl)amino]propoxy]-1-benzofuran-2-carboxylate
-
-
N-([4-[5-(2-methyl-1H-imidazol-1-yl)pentyl]phenyl]acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide
-
-
N-[(1R)-1-[3-(3-aminopropyl)-4-(2-cyclohexylethoxy)benzyl]-2-hydroxyethyl]-2-[4-[4-(2-methyl-1H-imidazol-1-yl)butyl]phenyl]acetamide
-
-
Octapeptide inhibitors with hydrophobic amino acid in position 2
-
-
-
SC-58272
-
peptidomimetic derived from the N-terminal sequence of the substrate ADP-ribosylation factor-2, i.e. Arf2p
additional information
-
overview: inhibition by glycylpeptides with varying amino acids at positions 2 to 8
-
additional information
-
inhibitor design and development, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
Gly-(diaminobutyrate-gamma-NH2-4-azido-3-iodosalicylamide)-L-Ala-L-Ala-L-Ser-S-Ala-L-Arg-L-Arg
-
-
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview: Km values for glycylpeptides with varying amino acids sequence, influence of amino acid residue type and substitutions on affinity
-
additional information
additional information
-
overview fatty acid analogs with various substituents
-
additional information
additional information
-
overview fatty acid analogs with various substituents
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki of several mutants for S-(2-oxo)-pentadecyl-CoA at 24 and 37°C
-
additional information
additional information
-
overview: Ki values for glycylpeptides with varying amino acids at positions 2 to 5
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
assay development, ELISA with biotinylated peptide substrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
about half-maximal activity above pH 9.0 and below pH 7.0, inactive at pH 6.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drops over a solution of 0.1 M ammonium acetate, 0.1 M sodium cacodylate, pH 6.4, 20°C, 20% polyethylene glycol 4000, protein 25 mg/ml, a few days, structure determination and analysis by X-ray diffraction of binary and ternary complexes of enzyme, peptide substrate or myristoyl-CoA and inhibitor
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A202T
-
site-directed mutagenesis, alterations of both peptide and myristoyl binding sites, 3 to 6fold increased Ki for S-(2-oxo)-pentadecyl-CoA and 6 to 9fold increased Ki for SC-58272
C217R
-
site-directed mutagenesis, 3 to 6fold increase in Ki for inhibitor SC-58272, selective alteration of the enzymes peptide binding site
D417V
-
site-directed mutagenesis, reduced activity, temperature-sensitive
D451K
-
site-directed mutagenesis, no functional complementation of enzyme deficient nmt1-181 mutant at 36°C
D451N
-
site-directed mutagenesis, no functional complementation of enzyme deficient nmt1-181 mutant at 36°C
E167K
-
site-directed mutagenesis, coexpression of wild-type with Asp451, functional complementation of enzyme deficient nmt1-181 mutant at 36°C
E293K
-
site-directed mutagenesis, coexpression of wild-type with Asp451, functional complementation of enzyme deficient nmt1-181 mutant at 36°C
F170A/L171A
-
site-directed mutagenesis, increased Ki for S-(2-oxo)-pentadecyl-CoA, increased Km for peptide substrate, altered enzyme conformation which modifies myristoyl-CoA polarization during catalytic reaction
F413S
-
site-directed mutagenesis, reduced activity, temperature-sensitive
K389I
-
site-directed mutagenesis, reduced activity, temperature-sensitive
L171S
-
site-directed mutagenesis, reduced activity, temperature-sensitive
L408S
-
site-directed mutagenesis, reduced activity, temperature-sensitive
L420S
-
site-directed mutagenesis, reduced activity, temperature-sensitive
N102T
-
site-directed mutagenesis, reduced activity, temperature-sensitive
N169L
-
site-directed mutagenesis, slightly increased Km for peptide substrate, altered kinetics
N169L/T205A
-
site-directed mutagenesis, increased Km for peptide substrate, altered kinetics
N426I
-
site-directed mutagenesis, mutation of myristoyl-binding site
V395D
-
site-directed mutagenesis, reduced activity, temperature-sensitive
additional information
additional information
-
temperature sensitive mutant strain nmt1-181, exchange of Gly to Asp, 10fold increased Km for myristoyl-CoA at 36°C
additional information
-
temperature sensitive mutant strain nmt1-181, exchange of Gly to Asp, 10fold increased Km for myristoyl-CoA at 36°C
additional information
-
C-terminal deletion mutants M454 and L455 produce a 300-400fold reduction in the chemical transformation rate, shift of the rate-limite of the process steps
additional information
-
disruption or deletion of nmt1-gene causes recessive lethality
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged recombinant wild-type and mutants from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli JM101, coexpression of each of the 4 homologous rat alpha subunits of the signal-transducing, heterotrimeric G proteins to determine in vivo interaction of the 2 enzymes, structural analysis
-
expression of His-tagged wild-type and mutants in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the automated assay can be used for proteomic studies to determine the myristoylation state of any protein
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
Towler, D.E.; Adams, S.P.; Eubanks, S.R.; Towery, D.S.; Jackson-Machelski, E.; Glaser, L.; Gordon, J.I.
Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase [published erratum appears in Proc Natl Acad Sci U S A 1987 Nov;84(21):7523]
Proc. Natl. Acad. Sci. USA
84
2708-2712
1987
Saccharomyces cerevisiae
Heuckeroth, R.O.; Towler, D.A.; Adams, S.P.; Glaser, L.; Gordon, J.I.
11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase
J. Biol. Chem.
263
2127-2133
1988
Saccharomyces cerevisiae, Triticum aestivum
Wiegand, R.C.; Carr, C.; Minnerly, J.C.; Pauley, A.M.; Carron, C.P.; Langner, C.A.; Duronio, R.J.; Gordon, J.I.
The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli
J. Biol. Chem.
267
8591-8598
1992
Candida albicans, Saccharomyces cerevisiae
Rudnick, D.A.; Rocque, W.J.; McWherter, C.A.; Toth, M.V.; Jackson-Machelski, E.; Gordon, J.I.
Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism
Proc. Natl. Acad. Sci. USA
90
1087-1091
1993
Saccharomyces cerevisiae
Wagner, A.P.; Retey, J.
Synthesis of myristoyl-carba(dethia)-coenzyme A and S-(3-oxohexadecyl)-coenzyme A, two potent inhibitors of myristoyl-CoA: protein N-myristoyltransferase
Eur. J. Biochem.
195
699-705
1991
Saccharomyces cerevisiae
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
Kishore, N.S.; Lu, T.; Knoll, L.J.; Katoh, A.; Rudnick, D.A.; Mehta, P.P.; Devadas, B.; Huhn, M.; Atwood, J.L.; Adams, S.P.; Gokel, G.W.; Gordon, J.I.
The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Analysis of myristic acid analogs containing oxygen, sulfur, double bonds, triple bonds, and/or an aromatic residue
J. Biol. Chem.
266
8835-8855
1991
Saccharomyces cerevisiae
Rudnick, D.A.; McWherter, C.A.; Rocaque, W.J.; Lennon, P.J.; Getman, D.P.; Gordon, J.I.
Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
J. Biol. Chem.
266
9732-9739
1991
Saccharomyces cerevisiae
Duronio, R.J.; Rudnick, D.A.; Adams, S.P.; Towler, D.A.; Gordon, J.I.
Analyzing the substrate specificity of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase by co-expressing it with mammalian G protein alpha subunits in Escherichia coli
J. Biol. Chem.
266
10498-10504
1991
Saccharomyces cerevisiae
Gordon, J.I.; Duronio, R.J.; Rudnick, D.A.; Adams, S.P.; Gokel, G.W.
Protein N-myristoylation
J. Biol. Chem.
266
8647-8650
1991
Saccharomyces cerevisiae, no activity in Escherichia coli
Rudnick, D.A.; McWherter, C.A.; Adams, S.A.; Ropson, I.J.; Duronio, R.J.; Gordon, J.I.
Structural and functional studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli. Evidence for an acyl-enzyme intermediate
J. Biol. Chem.
265
13370-13378
1990
Saccharomyces cerevisiae, no activity in Escherichia coli
Heuckeroth, R.O.; Jackson-Machelski, E.; Adams, S.P.; Kishore, N.S.; Huhn, M.; Katoh, A.; Lu, T.; Gokel, G.W.; Gordon, J.I.
Novel fatty acyl substrates for myristoyl-CoA:protein N-myristoyl-transferase
J. Lipid Res.
31
1121-1129
1990
Saccharomyces cerevisiae
Heuckeroth, R.O.; Glaser, L.; Gordon, J.I.
Heteroatom-substituted fatty acid analogs as substrates for N-myristoyltransferase: an approach for studying both the enzymology and function of protein acylation
Proc. Natl. Acad. Sci. USA
85
8795-8799
1988
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ405
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
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
Lu, T.; Li, Q.; Katoh, A.; Hernandez, J.; Duffin, K.; Jackson-Machelski, E.; Knoll, L.J.; Gokel, G.W.; Gordon, J.I.
The substrate specificity of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase. Polar probes of the enzyme's myristoyl-CoA recognition site
J. Biol. Chem.
269
5346-5357
1994
Saccharomyces cerevisiae
Zhang, L.; Jackson-Machelski, E.; Gordon, J.I.
Biochemical studies of Saccharomyces cerevisiae myristoyl-coenzyme A:protein N-myristoyltransferase mutants
J. Biol. Chem.
271
33131-33140
1996
Saccharomyces cerevisiae
Farazi, T.A.; Manchester, J.K.; Gordon, J.I.
Transient-state kinetic analysis of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase reveals that a step after chemical transformation is rate limiting
Biochemistry
39
15807-15816
2000
Saccharomyces cerevisiae (P14743), Saccharomyces cerevisiae
Farazi, T.A.; Manchester, J.K.; Waksman, G.; Gordon, J.I.
Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis
Biochemistry
40
9177-9186
2001
Saccharomyces cerevisiae
Takamune, N.; Hamada, H.; Sugawara, H.; Misumi, S.; Shoji, S.
Development of an enzyme-linked immunosorbent assay for measurement of activity of myristoyl-coenzyme A:protein N-myristoyltransferase
Anal. Biochem.
309
137-142
2002
Saccharomyces cerevisiae
Farazi, T.A.; Waksman, G.; Gordon, J.I.
Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis
Biochemistry
40
6335-6343
2001
Saccharomyces cerevisiae (P14743), Saccharomyces cerevisiae
Boisson, B.; Meinnel, T.
A continuous assay of myristoyl-CoA:protein N-myristoyltransferase for proteomic analysis
Anal. Biochem.
322
116-123
2003
Saccharomyces cerevisiae, Arabidopsis thaliana (Q9LTR9), Arabidopsis thaliana
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
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)
Bowyer, P.; Tate, E.; Leatherbarrow, R.; Holder, A.; Smith, D.; Brown, K.
N-myristoyltransferase: A prospective drug target for protozoan parasites
ChemMedChem
3
402-408
2008
Histoplasma capsulatum, Saccharomyces cerevisiae, Candida albicans, Cryptococcus neoformans, Leishmania major, Plasmodium falciparum, Trypanosoma brucei
EXTERNAL LINKS (specific for EC-Number 2.3.1.97)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
