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acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
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acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
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[Acs protein]-N6-acetyl-L-lysine609 + NAD+ + H2O
[Acs protein]-L-lysine609 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
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[histone H4]-N6-acetyl-L-lysine16 + NAD+ + H2O
[histone H4]-L-lysine16 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KGGAAc-KRHRKIL
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[p53 peptide]-N6-acetyl-L-lysine382 + NAD+ + H2O
[p53 peptide]-L-lysine382 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
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additional information
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additional information
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
?
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
?
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Nepsilon-lysine acetyltransferase PhnO specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. The enzyme shows a high degree of substrate specificity
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additional information
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
?
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
?
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
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the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
?
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the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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additional information
?
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the enzyme also acts as an aminoalkylphosphonate N-acetyltransferase, EC 2.3.1.380. Determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites
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evolution
YjaB is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity
evolution
Phno is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
YfiQ is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
evolution
Yiac is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity. Enzyme YfiQ can inhibit Escherichia coli cell migration in soft agar
physiological function
Nepsilon-lysine acetyltransferases (KATs) specifically transfer an acetyl group from AcCoA to Nepsilon-lysine residues on proteins. Posttranslational modifications, such as Nepsilon-lysine acetylation, regulate protein function. The enzymes show a high degree of substrate specificity. Enzyme YiaC can inhibit Escherichia coli cell migration in soft agar. Overexpression of enzyme mutant YiaC YF70A inhibits migration similarly to overexpression of wild-type YiaC
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
additional information
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism
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Y117A
site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YjaB-dependent acetylation compared to wild-type
Y117F
site-directed mutagenesis, mutation of the conserved catalytic amino acid does not alter YjaB-dependent acetylation compared to wild-type
E78A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation
F70A
site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YiaC-dependent acetylation compared to wild-type. Overexpression of YiaC YF70A inhibits cell migration similarly to overexpression of wild-type YiaC
Y115A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents YiaC-dependent acetylation. Mutant YiaC Y115A is unable to inhibit cell migration in contrast to the wild-type enzyme
Y128A
site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
additional information
generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains
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