Literature summary for 2.3.1.286 extracted from

Christensen, D.G.; Meyer, J.G.; Baumgartner, J.T.; DSouza, A.K.; Nelson, W.C.; Payne, S.H.; Kuhn, M.L.; Schilling, B.; Wolfe, A.J.
Identification of novel protein lysine acetyltransferases in Escherichia coli (2018), mBio, 9, e01905-18 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene patZ, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression in Escherichia coli strain BW25113	Escherichia coli
gene phnO, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression of wild-type and mutant enzymes in Escherichia coli strain BW25113	Escherichia coli
gene yiaC, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression of wild-type and mutant enzymes in Escherichia coli strain BW25113	Escherichia coli
gene yjaB, sequence comparisons and phylogenetic analysis, recombinant enzyme overexpression of wild-type and mutant enzymes in Escherichia coli strain BW25113	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E78A	site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation	Escherichia coli
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	Escherichia coli
additional information	generation and analysis of the DELTAackA pta yfiQ mutant lacking the two known mechanisms of protein acetylation, but residual acetylation remains	Escherichia coli
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	Escherichia coli
Y117A	site-directed mutagenesis, mutation of the conserved catalytic amino acid reduces YjaB-dependent acetylation compared to wild-type	Escherichia coli
Y117F	site-directed mutagenesis, mutation of the conserved catalytic amino acid does not alter YjaB-dependent acetylation compared to wild-type	Escherichia coli
Y128A	site-directed mutagenesis, mutation of the conserved catalytic amino acid prevents PhnO-dependent acetylation	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + [protein]-L-lysine	Escherichia coli	-	CoA + [protein]-N6-acetyl-L-lysine	-	?
additional information	Escherichia coli	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	?	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09163	-	-
Escherichia coli	P16691	-	-
Escherichia coli	P37664	-	-
Escherichia coli	P76594	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + [protein]-L-lysine	-	Escherichia coli	CoA + [protein]-N6-acetyl-L-lysine	-	?
additional information	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	Escherichia coli	?	-	-
additional information	determination of substrate specificity, method, detailed overview. Structural analysis of KAT and AcP-dependent acetylation sites	Escherichia coli	?	-	-
additional information	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	Escherichia coli	?	-	-

Synonyms

Synonyms	Comment	Organism
KAT	-	Escherichia coli
More	cf. EC 2.3.1.380	Escherichia coli
patZ	-	Escherichia coli
peptidyl-lysine N-acetyltransferase	UniProt	Escherichia coli
phnO	-	Escherichia coli
protein lysine acetyltransferase	-	Escherichia coli
YfiQ	-	Escherichia coli
YiaC	-	Escherichia coli
YjaB	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
acetyl-CoA	-	Escherichia coli

General Information

General Information	Comment	Organism
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli

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Release 2023.1 (January 2023)