2.3.1.258: N-terminal methionine Nalpha-acetyltransferase NatE
This is an abbreviated version!
For detailed information about N-terminal methionine Nalpha-acetyltransferase NatE, go to the full flat file.
Word Map on EC 2.3.1.258
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2.3.1.258
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auxiliary
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nt-acetylation
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bisubstrate
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n-acetyltransferase
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n-termini
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drug-induced
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tunnel
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chromatid
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sister
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acetylome
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nalpha-terminal
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co-translationally
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medicine
- 2.3.1.258
-
auxiliary
-
nt-acetylation
-
bisubstrate
- n-acetyltransferase
-
n-termini
-
drug-induced
-
tunnel
-
chromatid
-
sister
-
acetylome
-
nalpha-terminal
-
co-translationally
- medicine
Reaction
Synonyms
ARD1, EC 2.3.1.88, hNaa50, hNatA, MtRimI, N-terminal acetyltransferase E, NAA10, NAA15, Naa50, Naa50/San, Naa50p, Naa50p (NAT5/SAN) N-terminal acetyltransferase complex, Nalpha-acetyltransferase, NAT, NAT1, NAT5, NAT5/SAN, NatA, NatA/Naa50 complex, NatE, RimI, RimI acetyltransferase, Rv3420c, SAN, ScNaa50, ScNatA, SpNaa50, SpNatA
ECTree
2.3.1.258 N-terminal methionine Nalpha-acetyltransferase NatEAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.258 - N-terminal methionine Nalpha-acetyltransferase NatE
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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
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recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
additional information
generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
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generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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additional information
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generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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additional information
N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae
additional information
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N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae
additional information
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N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae
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additional information
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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
-
additional information
-
recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex
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