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acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein] + CoA
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-
?
acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-[protein] + CoA
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-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-lysyl-[protein] + CoA
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-
-
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?
acetyl-CoA + an N-terminal-L-methionyl-L-methionyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-methionyl-[protein] + CoA
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best substrate
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalanyl-L-tyrosyl-[Scc1 protein] + CoA
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-
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-
?
acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-phenylalany-[protein] + CoA
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-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-seryl-[protein] + CoA
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-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-threonyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
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-
-
-
?
acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-methionyl-L-valyl-[protein] + CoA
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-
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?
acetyl-CoA + MAAA
Nalpha-acetyl-MAAA + CoA
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-
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?
acetyl-CoA + MDAA
Nalpha-acetyl-MDAA + CoA
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-
-
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?
acetyl-CoA + MDELFRRR
Nalpha-acetyl-MDELFRRR + CoA
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-
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?
acetyl-CoA + MEAA
Nalpha-acetyl-MEAA + CoA
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-
-
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?
acetyl-CoA + MFAA
Nalpha-acetyl-MFAA + CoA
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-
-
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?
acetyl-CoA + MFGPERRR
Nalpha-acetyl-MFGPERRR + CoA
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-
-
?
acetyl-CoA + MGAA
Nalpha-acetyl-MGAA + CoA
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-
-
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?
acetyl-CoA + MHAA
Nalpha-acetyl-MHAA + CoA
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-
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?
acetyl-CoA + MIAA
Nalpha-acetyl-MIAA + CoA
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-
-
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?
acetyl-CoA + MIGPERRR
Nalpha-acetyl-MIGPERRR + CoA
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-
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?
acetyl-CoA + MKAA
Nalpha-acetyl-MKAA + CoA
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-
-
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?
acetyl-CoA + MKEEVRRR
Nalpha-acetyl-MKEEVRRR + CoA
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-
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?
acetyl-CoA + MLAA
Nalpha-acetyl-MLAA + CoA
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-
-
-
?
acetyl-CoA + MLALIRRR
Nalpha-acetyl-MLALIRRR + CoA
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-
-
?
acetyl-CoA + MLDPERRR
Nalpha-acetyl-MLDPERRR + CoA
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-
-
?
acetyl-CoA + MLGPEGGRWG
CoA + Ac-MLGPEGGRWG
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-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRP
acetyl-CoA + Nalpha-acetyl-MLGPEGGRWGRPVGRRRRP
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-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRPVRVYP
?
optimal in vitro substrate
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-
?
acetyl-CoA + MLGPERRR
Nalpha-acetyl-MLGPERRR + CoA
best substrate
-
-
?
acetyl-CoA + MLGTERRR
Nalpha-acetyl-MLGTERRR + CoA
-
-
-
?
acetyl-CoA + MLGTGRRR
Nalpha-acetyl-MLGTGRRR + CoA
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-
-
?
acetyl-CoA + MLLPERRR
Nalpha-acetyl-MLLPERRR + CoA
-
-
-
?
acetyl-CoA + MLRPERRR
Nalpha-acetyl-MLRPERRR + CoA
-
-
-
?
acetyl-CoA + MMAA
Nalpha-acetyl-MMAA + CoA
-
substrate with highest catalytic efficiency
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-
?
acetyl-CoA + MNAA
Nalpha-acetyl-MNAA + CoA
-
-
-
-
?
acetyl-CoA + MQAA
Nalpha-acetyl-MQAA + CoA
-
-
-
-
?
acetyl-CoA + MRAA
Nalpha-acetyl-MRAA + CoA
-
-
-
-
?
acetyl-CoA + MSAA
Nalpha-acetyl-MSAA + CoA
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-
-
-
?
acetyl-CoA + MTAA
Nalpha-acetyl-MMAA + CoA
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-
-
-
?
acetyl-CoA + MVAA
Nalpha-acetyl-MVAA + CoA
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-
-
-
?
acetyl-CoA + MWAA
Nalpha-acetyl-MWAA + CoA
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-
-
-
?
acetyl-CoA + MYAA
Nalpha-acetyl-MYAA + CoA
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-
-
-
?
acetyl-CoA + N-terminal L-methionyl-[ARYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[ARYFRR]
DP9 peptide (MARYFRR) is a substrate of NatE, a synthetic peptide
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-
ir
acetyl-CoA + N-terminal-L-methionyl-L-leucyl-glycyl-L-proline
N-terminal-Nalpha-acetyl-L-methionyl-L-leucyl-glycyl-L-proline + CoA
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-
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ir
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
additional information
?
-
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
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-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
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-
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?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
peptide substrate binding structure, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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Naa50p (Nat5/San) displays both protein Nalpha- and Nepsilon-acetyltransferase activity
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?
additional information
?
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Naa50p also possesses Nepsilon-autoacetylation activity
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?
additional information
?
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Naa50p also possesses Nepsilon-autoacetylation activity
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?
additional information
?
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no activity with peptides SESSRRR, SYSMRRR, and DDIARRR
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?
additional information
?
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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
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?
additional information
?
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the enzyme acetylates all MXAA peptides except for MPAA
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?
additional information
?
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complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
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additional information
?
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complex hNatE, comprising subunits Naa10 and Naa15 (NatA) and Naa50, is more active than hNAA50 alone
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed gainst peptide representing N-terminus of GroES. RimIMtb acetylates DP9 (NatE substrate) 2.1fold better than DPC (NatA substrate). RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins
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additional information
?
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the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
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additional information
?
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the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
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additional information
?
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the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE)
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additional information
?
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potential substrates that are less acetylated in strains lacking isoform Naa50 are: vacuolar morphogenesis protein 7, nuclear cap-binding protein subunit 2, 60S ribosomal protein L16-A, aromatic amino acid aminotransferase 1, tRNA guanosine-2'-O-methyltransferase TRM3, low specificity L-threonine aldolase
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?
additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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-
additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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-
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
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-
additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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-
additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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-
-
additional information
?
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-
N-terminal acetylation (NTA) is an irreversible protein modification
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evolution
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
evolution
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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 form 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
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
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.)
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.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
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.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
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.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
-
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 form 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.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
-
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 form 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
-
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.). SpNaa50 and ScNaa50 do not contain an optimal Q/RxxGxG/A consensus acetyl-CoA binding motif
-
evolution
-
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
-
evolution
-
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
-
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
malfunction
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
malfunction
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association. Deletion of ScNaa50 shows no phenotype, while Naa50 knockout in higher organisms has been shown to perturb sister chromatid cohesion
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
-
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association
-
malfunction
-
yeast Naa50 alone is defective in activity due to compromised substrate binding. Evolutionarily conserved Naa15 TY mutants can disrupt NatA-Naa50 association. Deletion of ScNaa50 shows no phenotype, while Naa50 knockout in higher organisms has been shown to perturb sister chromatid cohesion
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metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
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physiological function
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Naa50 promotes sister-chromatid cohesion and promotes binding of sororin to cohesin
physiological function
-
Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion during Drosophila wing development. The enzyme is required for the correct interaction between Scc1 and Smc3
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
-
the gene san is required in vivo for normal mitosis of different types of somatic cells. In addition, it is also important for the correct resolution of chromosomes. During oogenesis the gene san is not required for germ line 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 an irreversible protein modification
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 an irreversible protein modification
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
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
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 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
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
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
physiological function
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
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 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 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
-
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 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 form a stable complex through evolutionarily conserved interactions, yeast Naa50 alone is defective in activity due to compromised substrate binding, mechanism, overview
-
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
-
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 an irreversible protein modification
-
physiological function
-
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
-
physiological function
-
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
-
physiological function
-
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
-
physiological function
-
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
-
additional information
structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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
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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. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA
additional information
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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. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA
additional information
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the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
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the NatE enzyme complex is composed of the subunits Naa50 and Naa15
additional information
the NatE enzyme complex is composed of the subunits Naa50, Naa10, and Naa15
additional information
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the NatE enzyme complex is composed of the subunits Naa50 and Naa15
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additional information
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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
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additional information
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the NatE enzyme complex is composed of the subunits Naa50 and Naa15
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additional information
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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
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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. Shaped like a horseshoe, ScNaa15 of NatA is composed of 15 TPR motifs, which often mediate protein-protein interactions. The auxiliary subunit, consisting of a total 42 alpha-helices, serves as the binding scaffold for both catalytic subunits. ScNaa10 is completely wrapped by the Naa15 helices (from alpha11 to alpha30, encompassing residues Lys198-Gly595) with extensive interactions. Naa50 contacts both subunits of NatA
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additional information
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the NatE enzyme complex is composed of the subunits Naa50 and Naa15
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L814P
site-directed mutagenesis, the hNAA15 mutant is defective for HYPK inhibition and reduces hNatA thermostability, hNAA10 binding is not affected
T406Y
site-directed mutagenesis, the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected
Y124F
the mutant shows decreased activity compared to the wild type enzyme
F27A
site-directed mutagenesis, inactive mutant
F27A
the mutant shows less than 10% of wild type catalytic efficiency
F35A
site-directed mutagenesis, inactive mutant
F35A
the mutant shows less than 10% of wild type catalytic efficiency
H112A
inactive
H112A
site-directed mutagenesis, inactive mutant
H112A
NMR spectroscopy using the catalytically inactive hNaa50p mutant
H112A
the mutant shows less than 10% of wild type catalytic efficiency
H112F
site-directed mutagenesis, inactive mutant
H112F
the mutant shows less than 10% of wild type catalytic efficiency
I142A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I142A
the mutant shows 42.2% of wild type catalytic efficiency
P28A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P28A
the mutant shows less 13.4% of wild type catalytic efficiency
V29A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V29A
the mutant shows 12.3% of wild type catalytic efficiency
Y139A
site-directed mutagenesis, inactive mutant
Y139A
the mutant shows less than 10% of wild type catalytic efficiency
Y31A
site-directed mutagenesis, inactive mutant
Y31A
the mutant shows less than 10% of wild type catalytic efficiency
Y73A
site-directed mutagenesis, inactive mutant
Y73A
the mutant shows less than 10% of wild type catalytic efficiency
Y73F
site-directed mutagenesis, inactive mutant
Y73F
the mutant shows less than 10% of wild type catalytic efficiency
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
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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
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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)
brenda
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)
brenda
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)
brenda
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
Saccharomyces cerevisiae, Homo sapiens
brenda
Pimenta-Marques, A.; Tostoes, R.; Marty, T.; Barbosa, V.; Lehmann, R.; Martinho, R.
Differential requirements of a mitotic acetyltransferase in somatic and germ line cells
Dev. Biol.
323
197-206
2008
Drosophila melanogaster
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
Ribeiro, A.L.; Silva, R.D.; Foyn, H.; Tiago, M.N.; Rathore, O.S.; Arnesen, T.; Martinho, R.G.
Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion
Sci. Rep.
6
39118
2016
Drosophila melanogaster
brenda
Hou, M.; Zhuang, J.; Fan, S.; Wang, H.; Guo, C.; Yao, H.; Lin, D.; Liao, X.
Biophysical and functional characterizations of recombinant RimI acetyltransferase from Mycobacterium tuberculosis
Acta Biochim. Biophys. Sin. (Shanghai)
51
960-968
2019
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32), Mycobacterium tuberculosis ATCC 25618 (I6YG32)
brenda
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
brenda
Pathak, D.; Bhat, A.; Sapehia, V.; Rai, J.; Rao, A.
Biochemical evidence for relaxed substrate specificity of Nalpha-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis
Sci. Rep.
6
28892
2016
Mycobacterium tuberculosis (I6YG32), Mycobacterium tuberculosis H37Rv (I6YG32), Mycobacterium tuberculosis ATCC 25618 (I6YG32)
brenda
Lyon, G.
From molecular understanding to organismal biology of N-terminal acetyltransferases
Structure
27
1053-1055
2019
Schizosaccharomyces pombe, Saccharomyces cerevisiae (Q08689 AND P41227 AND P12945), Saccharomyces cerevisiae, Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Schizosaccharomyces pombe ATCC 24843, Schizosaccharomyces pombe 972, Saccharomyces cerevisiae ATCC 204508 (Q08689 AND P41227 AND P12945)
brenda
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
Schizosaccharomyces pombe, Saccharomyces cerevisiae (Q08689 AND P07347 AND P12945), Saccharomyces cerevisiae, Homo sapiens (Q9GZZ1 AND P41227 AND Q9BXJ9), Homo sapiens, Schizosaccharomyces pombe ATCC 24843, Schizosaccharomyces pombe 972, Saccharomyces cerevisiae ATCC 204508 (Q08689 AND P07347 AND P12945)
brenda