2.3.1.255: N-terminal amino-acid Nalpha-acetyltransferase NatA
This is an abbreviated version!
For detailed information about N-terminal amino-acid Nalpha-acetyltransferase NatA, go to the full flat file.
Word Map on EC 2.3.1.255
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2.3.1.255
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auxiliary
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n-acetyltransferase
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n-termini
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ogden
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co-translationally
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n-alpha-acetylation
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hypk
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cotranslation
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medicine
- 2.3.1.255
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auxiliary
- n-acetyltransferase
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n-termini
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ogden
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co-translationally
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n-alpha-acetylation
- hypk
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cotranslation
- medicine
Reaction
Synonyms
ARD homolog a, ARD1, ARD1-NAT1 Nalpha-acetyltransferase, ARD1131, ARD1198, ARD1225, ARD1235, Ard1b, ARD1p, ARD2, arrest defective 1, arrest-defective protein 1, arrest-defective protein 1 homologue, AtNAA10, daf-31, DXS707, EC 2.3.1.88, hARD1, hNaa10, hNaa15, hNaa16p, hNat2, More, MtRimI, MUSE6, N(alpha)-acetyltransferase 10, N-alpha-acetyltransferase, N-alpha-acetyltransferase 10, N-alpha-acetyltransferase 11, N-alpha-acetyltransferase 15, N-terminal acetyltransferase, N-terminal acetyltransferase 10, N-terminal acetyltransferase A, N-terminal protein acetyltransferase, NAA10, NAA10-NAA15, NAA10-NAA15 complex, NAA10-NAA15 protein complex, NAA10/ARD1, NAA11, NAA15, Nalpha-acetyltransferase, Nalpha-acetyltransferase 10, NAT, NAT1, NatA, NatA acetyltransferase, NatA Nalpha-terminal acetyltransferase, NatA protein complex, NatA protein Nalpha-terminal-acetyltransferase complex, RimI, RimI acetyltransferase, Rv3420c, SCNaa15, ScNatA, SpNaa10, SpNaa15, SSO0209, Ta0058, Ta1140, TbARD1, TcNatA, TE2, vnc, yNaa10, yNaa15, zNaa10
ECTree
2.3.1.255 N-terminal amino-acid Nalpha-acetyltransferase NatAAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.255 - N-terminal amino-acid Nalpha-acetyltransferase NatA
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F128I
site-directed mutagenesis, the mutation leads an altered structure and reduced stability, and a dramatic recuction of Nt catalytic activity compared to wild-type
F128L
site-directed mutagenesis, the mutation leads an altered structure and reduced stability, and a dramatic recuction of Nt catalytic activity compared to wild-type
I72T
a naturally occuring mutation NAA10 c.215T>C, the mutant phenotype shows a milder phenotypic spectrum in comparison to most of the previously described patients with NAA10 variants. The three boys have development delay, intellectual disability, and cardiac abnormalities as overlapping phenotypes. NAA10 Ile72Thr protein is destabilized, while binding to NAA15 most likely is intact. The NatA activity of NAA10 Ile72Thr appears normal while its monomeric activity is decreased. Genotype-phenotype correlations for NAA10 variants, overview
K136R
L814P
P41227; Q9BXJ9
site-directed mutagenesis, the hNAA15 mutant is defective for HYPK inhibition and reduces hNatA thermostability, hNAA10 binding is not affected. The hNAA15-L814P-V5 hNatA complex shows an increased catalytic activity compared to wild-type hNatA
R116W
site-directed mutagenesis, the mutation leads to a reduction in catalytic activity for the peptide substrates EEEI and SESS by 15% compared to wild-type
R82A/Y122F
R83C
site-directed mutagenesis, the mutation interferes with acetyl-CoA binding and leads to a 60% reduction in Nt-catalytic activity compared to wild-type
R83H
P41227; Q9BXJ9
naturally occuring c.248G > A missense mutation, reduced enzymatic activity of monomeric NAA10-R83H. This variant is modelled to have an altered charge density in the acetyl-CoA binding region of NAA10
S37P
T406Y
P41227; Q9BXJ9
site-directed mutagenesis, the hNAA15-T406Y-V5 hNatA mutant complex displays a decreased catalytic activity toward the hNatA substrate SESS compared to wild-type hNatA. the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected
V107F
site-directed mutagenesis, the mutation leads to a reduction in catalytic activity for the peptide substrates EEEI and SESS by 95% compared to wild-type
V111G
P41227; Q9BXJ9
a naturally occuring 332 T > G missense mutant, the mutant Naa10 has a reduced stability and 85% reduced monomeric catalytic activity, while catalytic NatA function remains unaltered. NAA10-V111G has a reduced stability compared to wild-type NAA10, and in vitro acetylation assays reveal a reduced enzymatic activity of monomeric NAA10-V111G but not for NAA10-V111G in complex with NAA15 (NatA enzymatic activity). A glycine in position 111 instead of valine will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or acetyl-CoA binding
Y43S
site-directed mutagenesis, the mutant is catalytically impaired in vitro, with approximately an 85% reduction in Nt-catalytic activity for peptide substrates EEEI, DDDI, and SESS
N132A
the mutant shows 4.5fold increase in Km, with no significant difference in kcat compared to the wild type enzyme
R100A
the mutant shows 7fold increase in Km, with no significant difference in kcat compared to the wild type enzyme
T105A
the mutant shows 3fold increase in Km, with no significant difference in kcat compared to the wild type enzyme
S39P
E24A
mutation in NatA, decrease in kcat, increase in Km value
E24D
mutation in NatA, decrease in kcat, increase in Km value
E24Q
mutation in NatA, decrease in kcat, increase in Km value
E61A
mutation in NatA, decrease in kcat, increase in Km value
E62A
mutation in NatA, decrease in kcat, increase in Km value
H111A
mutation in NatA, decrease in kcat, Km value similar to wild-type
H20A
mutation in NatA, decrease in kcat, increase in Km value
H72A
mutation in NatA, decrease in kcat, increase in Km value
K29A
mutation in NatA, increase in kcat, decrease in Km value
K29A/Y33A
mutation in NatA, decrease in kcat, Km value similar to wild-type
K59A
mutation in NatA, decrease in kcat, increase in Km value
K59A/E61A
mutation in NatA, decrease in kcat, increase in Km value
K59A/E62A
mutation in NatA, decrease in kcat, increase in Km value
L22A
mutation in NatA, decrease in kcat, increase in Km value
P23A
mutation in NatA, decrease in kcat, increase in Km value
R113A
mutation in NatA, strong decrease in kcat, Km value similar to wild-type
R80A
mutation in NatA, decrease in kcat, increase in Km value
Y26A
mutation in NatA, decrease in kcat, increase in Km value
Y33A
mutation in NatA, decrease in kcat, increase in Km value
additional information
K136R
site-directed mutagenesis, that lacks autoacetylation, the mutant shows wild-type NAT activity
K136R
site-directed mutagenesis, the non-acetylated K136R mutant shows N-terminal acetyltransferase capacity as strongly as the hARD1/NAA10 wild-type, but fails to acetylate itself
R82A/Y122F
site-directed mutagenesis, the mutant shows highly reduced NAT activity compared to wild-type
R82A/Y122F
the acetyltransferase dead DN mutant of hARD1/NAA10 almost loses its NAT activity and fails to acetylate itself. The DN mutant includes two mutations R82A and Y122F, which inhibit the binding of acetyl-CoA to hARD1/NAA10 and consequently suppresses its acetyltransferase activity
S37P
site-directed mutagenesis, the mutant Naa10 protein shows reduced catalytic activity for EEEI, DDDI, and SESS peptide substrates, and inability to combine with Naa15. The mutant hNaa10 S37P recombinantly expressed in a NatA-defective Saccharomyces cerevisiae strain lacks a proper complex formation with hNaa15 and is reduced in in vitro catalytic activity
S39P
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site-directed mutagenesis, the mutation does not cause a phenotype
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additional information
generation of mutant naa10-1 and of a naa15 mutant by T-DNA insertion-disrupting gene expression
additional information
enzyme knockdown by siRNA. Generation of mutant daf-31(m655) by removal of 151 bp of promoter upstream of the ATG start codon and 242 bp of daf-31 coding region dowstream of the ATG start codon. Generation of and overexpression mutant daf-31 OE for which the full-length dar-31 genomic DNA is cloned into pGEM-T vector. Generation of mutant vncBDk by with impaired N-terminal activity
additional information
Caenorhabditis elegans DAF-31
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enzyme knockdown by siRNA. Generation of mutant daf-31(m655) by removal of 151 bp of promoter upstream of the ATG start codon and 242 bp of daf-31 coding region dowstream of the ATG start codon. Generation of and overexpression mutant daf-31 OE for which the full-length dar-31 genomic DNA is cloned into pGEM-T vector. Generation of mutant vncBDk by with impaired N-terminal activity
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additional information
generation of mutant naa10MO by morpholino-based knockdown
additional information
generation of enzyme mutant by frame shift mutation causing a acetyltransferase-truncated enzymatic region, and of another mutant vnc by intron-insertion mutation
additional information
construction of Naa10 stably knocked down H1299 cell line H1299-shNaa10, cDNA microarray analysis
additional information
knockdown of Naa10p by shRNAs, knockdown efficiencies, overview. Generation of truncated Naa10p mutants
additional information
silencing of mouse immortalized embryonic endothelial cells
additional information
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silencing of mouse immortalized embryonic endothelial cells
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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
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
P07347; P12945
mutation ard1::HIS3 is caused by inserting a Barn HI fragment containinng the HIS3 gene into the Barn HI site of plasmid YCpE18 that lies within the functional sequence of ARD1. Genes nat1/ard1 double mutant nat1-5::LEU;ard1 is generated by mating of nat1 and ard1 single mutants, the single mutants of nat1 (Naa15) and ard1 (Naa10) display identical phenotypes, no additional phenotypes are found in the double mutant. Recombinant expression of the S37P mutant of human Naa10 in a NatA-defective yeast strain, the hNaa10 expressing mutant strain shows a lack of proper complex formation with hNaa15 and reduced in vitro catalytic activity, a decrease of Nt-acetylome and an increase in the Hsp70 family proteins
additional information
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mutation ard1::HIS3 is caused by inserting a Barn HI fragment containinng the HIS3 gene into the Barn HI site of plasmid YCpE18 that lies within the functional sequence of ARD1. Genes nat1/ard1 double mutant nat1-5::LEU;ard1 is generated by mating of nat1 and ard1 single mutants, the single mutants of nat1 (Naa15) and ard1 (Naa10) display identical phenotypes, no additional phenotypes are found in the double mutant. Recombinant expression of the S37P mutant of human Naa10 in a NatA-defective yeast strain, the hNaa10 expressing mutant strain shows a lack of proper complex formation with hNaa15 and reduced in vitro catalytic activity, a decrease of Nt-acetylome and an increase in the Hsp70 family proteins
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additional information
generation of an Ard1 null mutant by removal of the ARD1 coding region
