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Information on EC 2.3.1.258 - N-terminal methionine Nalpha-acetyltransferase NatE and Organism(s) Homo sapiens and UniProt Accession P41227
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2.3.1.258 N-terminal methionine Nalpha-acetyltransferase NatEIUBMB Comments
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nalpha-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.
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Word Map
- 2.3.1.258
-
auxiliary
-
nt-acetylation
-
bisubstrate
- n-acetyltransferase
-
n-termini
-
drug-induced
-
tunnel
-
chromatid
-
sister
-
acetylome
-
nalpha-terminal
-
co-translationally
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
naa50, hnata, hnaa50, naa50/san, scnaa50, nata/naa50 complex, n-terminal acetyltransferase e, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Naa50
Naa50p
NAT5
NatA
NatE
SAN
Naa50
-
-
-
-
NAT5
-
-
-
-
SAN
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
hNaa50p utilizes an ordered bi bi reaction of the Theorell-Chance type, substarte binding study and dynamics using NMR spectroscopy. Acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site. Addition of peptide in the absence of acetyl-CoA does not alter the structure of the protein
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nalpha-acetyltransferase
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nalpha-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.
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
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
-
best substrate
-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRP
acetyl-CoA + Nalpha-acetyl-MLGPEGGRWGRPVGRRRRP
-
-
-
?
acetyl-CoA + MMAA
Nalpha-acetyl-MMAA + CoA
-
substrate with highest catalytic efficiency
-
-
?
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
-
-
-
ir
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
peptide substrate binding structure, overview
-
-
?
additional information
?
-
-
ectopically expressed hNaa50 results, predominantly, in the N-terminal-acetylation of N-terminal Met (iMet) starting N-termini, including iMet-Lys, iMet-Val, iMet-Ala, iMet-Tyr, iMet-Phe, iMet-Leu, iMet-Ser, and iMet-Thr N-termini. Presence of a kinetic competition between Naa50 and Met-aminopeptidases
-
-
?
additional information
?
-
Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
-
-
?
additional information
?
-
-
Naa50p also possesses Nepsilon-autoacetylation activity
-
-
?
additional information
?
-
Naa50p also possesses Nepsilon-autoacetylation activity
-
-
?
additional information
?
-
no activity with peptides SESSRRR, SYSMRRR, and DDIARRR
-
-
?
additional information
?
-
preferably the enzyme acetylates oligopeptides with N-termini Met-Leu-Xxx-Pro. Furthermore, the enzyme autoacetylates lysines 34, 37, and 140 in vitro as well as histone 4
-
-
?
additional information
?
-
-
the enzyme acetylates all MXAA peptides except for MPAA
-
-
?
additional information
?
-
complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
-
-
-
additional information
?
-
-
complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
-
-
-
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
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
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
-
best substrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HYPK
UniProt ID Q9NX55, a protein with intrinsic NAA10 catalytic subunit inhibitory activity. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex. hNatE displays an about 8.6fold decrease of Km, and an about 1.1fold decrease of kcat, with an overall 7.7fold increase of catalytic efficiency, compared to hNAA50. In the presence HYPK, hNatE displays an about 1.3fold decrease in Km, and an about 3.8fold decrease in kcat, with an overall 2.9fold decrease in catalytic efficiency compared to hNatE alone. The hNatE/HYPK structure reveals a negative cooperative mechanism. Over the HYPK and hNatA interaction interface within the tetrameric complex, polar interactions between HYPK-Glu74 and hNAA15-Tyr158, between the backbone carbonyl of HYPK-Thr100 and hNAA15-Lys687, between the backbone carbonyl of HYPK-Asn129 and hNAA15-Arg697, and between HYPK-Asn129 and hNAA15-Lys696 are observed
-
CoA
product inhibition, competitive versus acetyl-CoA, noncompetitive against peptide substrate well in line with a ternary complex mechanism. The non-competitive inhibition pattern observed when CoA is tested against peptide as variable substrate and at fixed concentrations of acetyl-CoA also rules out a ping-pong mechanism
additional information
NAA50 and HYPK each contribute to NAA10 activity inhibition through structural alteration of the NAA10 substrate-binding site. NAA50 activity is increased through NAA15 tethering, but is inhibited by HYPK through structural alteration of the NatE substrate-binding site. hNAA50 and HYPK inhibit hNatA activity, and HYPK is dominant. The hNatE structure reveals molecular basis for enzyme crosstalk
-
additional information
-
NAA50 and HYPK each contribute to NAA10 activity inhibition through structural alteration of the NAA10 substrate-binding site. NAA50 activity is increased through NAA15 tethering, but is inhibited by HYPK through structural alteration of the NatE substrate-binding site. hNAA50 and HYPK inhibit hNatA activity, and HYPK is dominant. The hNatE structure reveals molecular basis for enzyme crosstalk
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NAA50 activity is increased through NAA15 tethering. hNatA significantly enhances the catalytic efficiency of hNatE
-
additional information
-
NAA50 activity is increased through NAA15 tethering. hNatA significantly enhances the catalytic efficiency of hNatE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0962
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNatE, pH 8.5, 37°C
0.8315
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNaa50, pH 8.5, 37°C
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
binding kinetics of hNaa50 and hNatA, Naa50 tightly binds to NatA
-
additional information
additional information
-
binding kinetics of hNaa50 and hNatA, Naa50 tightly binds to NatA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0515
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNatE, pH 8.5, 37°C
0.0575
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNaa50, pH 8.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.069
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNaa50, pH 8.5, 37°C
0.535
N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
recombinant hNatE, pH 8.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00227
CoA
with acetyl-CoA, pH 7.4, temperature not specified in the publication
0.00277
CoA
with peptide, pH 7.4, temperature not specified in the publication
0.067
desulfo-CoA
with acetyl-CoA, pH 7.4, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
physiological function
additional information
evolution
the crystal structure of yeast NatA/Naa50 is used as a scaffold to uncover evolutionarily conserved catalytic crosstalk within the orthologous complexes in yeast and human, overview. NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding. The Saccharomyces cerevisiae ScNaa15 auxiliary subunit of NatA displays a high degree of structure conservation with Schizosaccharomyces pombe SpNaa15 and human hNaa15. NatA-Naa50 from yeast and human make conserved interactions
evolution
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
malfunction
-
depletion of Naa50 in HeLa cells causes cohesion defects in interphase
malfunction
enzyme depletion causes premature sister chromatid separation in HeLa cells
malfunction
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
physiological function
-
Naa50 promotes sister-chromatid cohesion and promotes binding of sororin to cohesin
physiological function
the acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner. The enzyme is specifically required for the maintenance of the centromeric cohesion in mitosis
physiological function
enzyme complex NatE co-translationally acetylates the N-terminus of half the proteome to mediate diverse biological processes, including protein half-life, localization, and interaction. The complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
physiological function
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is estimated to affect up to 90% of human proteins and influences their folding, localization, complex formation, and degradation, along with a variety of cellular functions ranging from apoptosis to gene regulation. NTA is an irreversible protein modification
physiological function
NatA (EC 2.3.1.255) co-translationally acetylates the N-termini of over 40% of eukaryotic proteins and can associate with another catalytic subunit, Naa50, to form a ternary NatA/Naa50 dual enzyme complex (also called NatE). NatA/Naa50 forms a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
additional information
the human N-terminal acetyltransferase E (NatE) contains NAA10 and NAA50 as catalytic subunits, and NAA15 auxiliary as subunit and associates with HYPK, a protein with intrinsic NAA10 inhibitory activity. hNatE and inhibitor HYPK form a tetrameric complex. Analysis of the molecular basis for how NatE and HYPK cooperate, cryo-EM structures of human NatE and NatE/HYPK complexes, overview. NAA50 and HYPK exhibit negative cooperative binding to NAA15 in vitro and in human cells by inducing NAA15 shifts in opposing directions. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex
additional information
-
the human N-terminal acetyltransferase E (NatE) contains NAA10 and NAA50 as catalytic subunits, and NAA15 auxiliary as subunit and associates with HYPK, a protein with intrinsic NAA10 inhibitory activity. hNatE and inhibitor HYPK form a tetrameric complex. Analysis of the molecular basis for how NatE and HYPK cooperate, cryo-EM structures of human NatE and NatE/HYPK complexes, overview. NAA50 and HYPK exhibit negative cooperative binding to NAA15 in vitro and in human cells by inducing NAA15 shifts in opposing directions. HYPK and hNAA50 can bind to hNatA simultaneously to form a tetrameric hNatE/HYPK complex
additional information
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
additional information
-
the NatA/Naa50 complex contains two catalytic subunits and one auxiliary subunit for co-translational N-terminal acetylation, structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex, overview. NatA-Naa50 interactions promote catalytic crosstalk between Naa10 and Naa50
additional information
the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to a native substrate peptide fragment (MLGPEGGRWG) and CoA, hanging drop vapor diffusion method, using 16% (w/v) PEG 8000, 20% (v/v) glycerol, and 40 mM potassium phosphate (monobasic, pH 5.0)
hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M sodium formate
-
Naa50p bound to a native substrate peptide fragment and CoA, hanging drop vapor diffusion method, mixing of 12 mg/ml protein in 25 mM HEPES, pH 7.5, 100 mM NaCl, and 10mM dithiothreitol, with peptide MLGPEGGRWG solution, and crystallization solution, containing 16% PEG 8000, 20% glycerol, and 40 mM potassium phosphate, pH 5.0, in a 1:3:3 molar ratio, 20°C, 1-3 days, X-ray diffraction structure determination and analysis at 2.75 A resolution
purified hNatE and hNatE in complex with inhibitor HYPK, X-ray diffraction structure determination and analysis at 4.5-5.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F27A
F35A
H112A
H112F
I142A
L814P
site-directed mutagenesis, the hNAA15 mutant is defective for HYPK inhibition and reduces hNatA thermostability, hNAA10 binding is not affected
P28A
T406Y
site-directed mutagenesis, the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected
V29A
Y124F
the mutant shows decreased activity compared to the wild type enzyme
Y139A
Y31A
Y73A
Y73F
additional information
I142A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P28A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V29A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
additional information
-
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged full-length Naa50p from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography and cleavage of the GST-tag by TEV protease, followed by ion exchange chromatography and gel filtration
recombinant GST-tagged hNaa50 and hNatA fromSf9 insect cells by affinity chromatography and gel filtration
recombinant hNaa15 mutants, hNaa50, and hNatA by affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression of GST-tagged full-length Naa50p with a TEV protease-cleavable site in Escherichia coli strain BL21(DE3)
recombinant expression of hNaa15 mutants in HeLa cells, recombinant expression of N-terminally His-tagged NatA in Spodoptera frugiperda Sf9 cells, recombinant expression of His-tagged hNaa50 in Escherichia coli strain Rosetta (DE3)pLysS and strain BL21(DE3), coexpression of tagged HYPK
recombinant overexpression of GST-tagged hNaa50 and hNatA in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
Naa50p is a therapeutic anti-cancer target, the structure of the ternary Naa50p complex also provides a molecular scaffold for the design of NAT-specific small molecule inhibitors with possible therapeutic applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arnesen, T.; Anderson, D.; Torsvik, J.; Halseth, H.B.; Varhaug, J.E.; Lillehaug, J.R.
Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex
Gene
371
291-295
2006
Homo sapiens (Q9GZZ1)
Liszczak, G.; Arnesen, T.; Marmorsteins, R.
Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation
J. Biol. Chem.
286
37002-37010
2011
Homo sapiens, Homo sapiens (Q9GZZ1)
Evjenth, R.H.; Brenner, A.K.; Thompson, P.R.; Arnesen, T.; Fr?ystein, N.A.; Lillehaug, J.R.
Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study
J. Biol. Chem.
287
10081-10088
2012
Homo sapiens, Homo sapiens (Q9GZZ1)
Van Damme, P.; Hole, K.; Gevaert, K.; Arnesen, T.
N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases
Proteomics
15
2436-2446
2015
Homo sapiens, Saccharomyces cerevisiae
Evjenth, R.; Hole, K.; Karlsen, O.; Ziegler, M.; Amesen, T.; Lillehaug, J.
Human Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
J. Biol. Chem.
284
31122-31129
2009
Homo sapiens (Q9GZZ1)
Rong, Z.; Ouyang, Z.; Magin, R.S.; Marmorstein, R.; Yu, H.
Opposing functions of the N-terminal acetyltransferases Naa50 and NatA in sister-chromatid cohesion
J. Biol. Chem.
291
19079-19091
2016
Homo sapiens
Reddi, R.; Saddanapu, V.; Chinthapalli, D.; Sankoju, P.; Sripadi, P.; Addlagatta, A.
Human Naa50 protein displays broad substrate specificity for amino-terminal acetylation: Detailed structural and biochemical analysis using tetrapeptide library
J. Biol. Chem.
291
20530-20538
2016
Homo sapiens
Hou, F.; Chu, C.; Kong, X.; Yokomori, K.; Zou, H.
The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner
J. Cell Biol.
177
587-597
2007
Homo sapiens (Q9GZZ1)
Deng, S.; McTiernan, N.; Wei, X.; Arnesen, T.; Marmorstein, R.
Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK
Nat. Commun.
11
818
2020
Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Homo sapiens
Lyon, G.
From molecular understanding to organismal biology of N-terminal acetyltransferases
Structure
27
1053-1055
2019
Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Saccharomyces cerevisiae (Q08689 AND P41227 AND P12945), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q08689 AND P41227 AND P12945), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972, Schizosaccharomyces pombe ATCC 24843
Deng, S.; Magin, R.; Wei, X.; Pan, B.; Petersson, E.; Marmorstein, R.
Structure and mechanism of acetylation by the N-terminal dual enzyme NatA/Naa50 complex
Structure
27
1057-1070.e4
2019
Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Homo sapiens, Saccharomyces cerevisiae (Q08689 AND P07347 AND P12945), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q08689 AND P07347 AND P12945), Schizosaccharomyces pombe, Schizosaccharomyces pombe 972, Schizosaccharomyces pombe ATCC 24843
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