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acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
acetyl-CoA + [acetyl coenzyme A synthase Mxan_2570]-L-lysine622
CoA + N-acetyl-[acetyl coenzyme A synthase Mxan_2570]-L-lysine622
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
acetyl-CoA + [AcsA]-L-Lys
CoA + [SaAcsA]-N6-acetyl-L-Lys
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
acetyl-CoA + [BtyA]-L-Lys
CoA + [BtyA]-N6-acetyl-L-Lys
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substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaA]-L-Lys
CoA + [DcaA]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaB]-L-Lys
CoA + [DcaB]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaC]-L-Lys
CoA + [DcaC]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [GapA]-L-Lys
CoA + [GapA]-N6-acetyl-L-Lys
ACS is glyceraldehyde-3-phosphate dehydrogenase
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?
acetyl-CoA + [LcsB mutant L500V]-L-Lys
CoA + [LcsB mutant L500V]-N6-acetyl-L-Lys
-
wild-type AMP-forming acyl-CoA synthase LcsB is not a substrate, acetylation of mutant L500V occurs at the catalytic lysine residue
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?
acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
acetyl-CoA + [PimA]-L-Lys534
CoA + [PimA]-N6-acetyl-L-Lys534
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substrate is a AMP-forming acyl-CoA synthase
alanine substitutions at residues Pro528, Arg529, Thr530, Val532, and Gly533 of PimA result in variants that are acetylated less than 50% relative to the wild-type protein. C-terminal to the acetylation site, alanine substitutions at residues Arg537, Leu540, and Arg541 yield variants that also showed less than 50% of wild-type acetylation
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
acetyl-CoA + [VcsA]-L-Lys
CoA + [VcsA]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
propionyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-propionyl-L-Lys
propionyl-CoA + [PprE]-L-Lys
CoA + [PprE]-N6-propionyl-L-Lys
PprE is propionyl-CoA synthetase
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-
?
succinyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-succinyl-L-Lys
additional information
?
-
acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
-
substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617
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?
acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
-
substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617
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?
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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-
?
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
ACS is isocitrate dehydrogenase kinase
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?
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
ACS is isocitrate dehydrogenase kinase
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?
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
ACS is isocitrate dehydrogenase kinase
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
enzyme is responsible for the acetylation of the AMP-forming acetyl coenzyme A synthase AcsA, i.e.SACE_2375. Acetylation occurs at residues Lys237, Lys380, Lys611, and Lys628
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
enzyme is responsible for the acetylation of the AMP-forming acetyl coenzyme A synthase AcsA, i.e.SACE_2375. Acetylation occurs at residues Lys237, Lys380, Lys611, and Lys628
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs)
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs), lysine residue K546 is acetylated
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs)
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-
?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs), lysine residue K546 is acetylated
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [SaAcsA]-N6-acetyl-L-Lys
SaAcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus, lysine residue K546 is acetylated
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [SaAcsA]-N6-acetyl-L-Lys
SaAcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus, lysine residue K546 is acetylated
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
-
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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r
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is AcCoA synthase, Nepsilon-lysine-acetylation
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is isocitrate lyase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is AcCoA synthase, Nepsilon-lysine-acetylation
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is AcCoA synthase, Nepsilon-lysine-acetylation
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
-
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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r
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
-
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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-
?
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis
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-
?
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis
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-
?
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis(BsAcsA)
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-
?
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis(BsAcsA)
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?
acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
substrate is acetyl-CoA synthase Micau_0428. substrate mutant K619 is not acetylated
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?
acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
substrate is acetyl-CoA synthase Micau_0428. substrate mutant K619 is not acetylated
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is AMP-forming acetyl-CoA synthetase from Salmonella enterica
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is AMP-forming acetyl-CoA synthetase from Salmonella enterica
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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-
?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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-
?
propionyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-propionyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs)
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-
?
propionyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-propionyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs), lysine residue K546 is propionylated
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?
succinyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-succinyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs). AcuA is the first documented case of a bacterial GNAT capable of succinylation
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?
succinyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-succinyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs). AcuA is the first documented case of a bacterial GNAT capable of succinylation, lysine residue K546 is succinylated
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?
additional information
?
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enzyme BsAcuA acetylates BsAcsA and also SaAcsA from Staphylococcus aureus, as well as SeAcs from Salmonella enterica
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additional information
?
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enzyme BsAcuA acetylates BsAcsA and also SaAcsA from Staphylococcus aureus, as well as SeAcs from Salmonella enterica
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additional information
?
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enzyme inactivates AMP-forming acyl-CoA synthases by acetylating the epsilon-amino group of a conserved, catalytic lysine residue. Substrate recognition motif is PK/RTXS/T/V/NGKX2K/R. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. No substrate: long-chain acyl-CoA synthase B
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?
additional information
?
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SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)
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additional information
?
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enzyme SePat acetylates SeAcs, but it fails to acetylate AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) and Bacillus subtilis (BsAcsA)
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additional information
?
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the NDP-forming AcCoA domain is unable to produce acetyl-CoA from acetate, ATP, and CoA because the catalytic histidine, present e.g. in Escherichia coli PatZ, is replaced with an asparagine (N114) in SePat
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additional information
?
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enzyme SePat acetylates SeAcs, but it fails to acetylate AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) and Bacillus subtilis (BsAcsA)
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additional information
?
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SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)
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additional information
?
-
the NDP-forming AcCoA domain is unable to produce acetyl-CoA from acetate, ATP, and CoA because the catalytic histidine, present e.g. in Escherichia coli PatZ, is replaced with an asparagine (N114) in SePat
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additional information
?
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enzyme SePat acetylates SeAcs, but it fails to acetylate AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) and Bacillus subtilis (BsAcsA)
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additional information
?
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SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)
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additional information
?
-
the NDP-forming AcCoA domain is unable to produce acetyl-CoA from acetate, ATP, and CoA because the catalytic histidine, present e.g. in Escherichia coli PatZ, is replaced with an asparagine (N114) in SePat
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additional information
?
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no activity with AcsA substrate mutants SaAcsK546A, SaAcsK546R, and SaAcsK546Q by SaAcuA. SaAcuA does not acetylate any of the K546 variants. Malonyl-CoA is a poor substrate of SaAcuA
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additional information
?
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no activity with AcsA substrate mutants SaAcsK546A, SaAcsK546R, and SaAcsK546Q by SaAcuA. SaAcuA does not acetylate any of the K546 variants. Malonyl-CoA is a poor substrate of SaAcuA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
acetyl-CoA + [BtyA]-L-Lys
CoA + [BtyA]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaA]-L-Lys
CoA + [DcaA]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaB]-L-Lys
CoA + [DcaB]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [DcaC]-L-Lys
CoA + [DcaC]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
acetyl-CoA + [LcsB mutant L500V]-L-Lys
CoA + [LcsB mutant L500V]-N6-acetyl-L-Lys
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wild-type AMP-forming acyl-CoA synthase LcsB is not a substrate, acetylation of mutant L500V occurs at the catalytic lysine residue
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?
acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
acetyl-CoA + [PimA]-L-Lys534
CoA + [PimA]-N6-acetyl-L-Lys534
-
substrate is a AMP-forming acyl-CoA synthase
alanine substitutions at residues Pro528, Arg529, Thr530, Val532, and Gly533 of PimA result in variants that are acetylated less than 50% relative to the wild-type protein. C-terminal to the acetylation site, alanine substitutions at residues Arg537, Leu540, and Arg541 yield variants that also showed less than 50% of wild-type acetylation
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?
acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
acetyl-CoA + [VcsA]-L-Lys
CoA + [VcsA]-N6-acetyl-L-Lys
-
substrate is a AMP-forming acyl-CoA synthase, acetylation occurs at the catalytic lysine residue
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-
?
propionyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-propionyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs)
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-
?
propionyl-CoA + [PprE]-L-Lys
CoA + [PprE]-N6-propionyl-L-Lys
PprE is propionyl-CoA synthetase
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?
succinyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-succinyl-L-Lys
AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs). AcuA is the first documented case of a bacterial GNAT capable of succinylation
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?
additional information
?
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acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
-
substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617
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?
acetyl-CoA + [AacS]-L-Lys617
CoA + [AacS]-Nepsilon-acetyl-L-Lys617
-
substrate acetoacetyl-CoA synthase AACS. Acetylation occurs at active site residue Lys617
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?
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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-
?
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [AceA]-L-Lys
CoA + [AceA]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
ACS is isocitrate dehydrogenase kinase
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?
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
ACS is isocitrate dehydrogenase kinase
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?
acetyl-CoA + [AceK]-L-Lys
CoA + [AceK]-N6-acetyl-L-Lys
ACS is isocitrate dehydrogenase kinase
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-
?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
enzyme is responsible for the acetylation of the AMP-forming acetyl coenzyme A synthase AcsA, i.e.SACE_2375. Acetylation occurs at residues Lys237, Lys380, Lys611, and Lys628
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-
?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
enzyme is responsible for the acetylation of the AMP-forming acetyl coenzyme A synthase AcsA, i.e.SACE_2375. Acetylation occurs at residues Lys237, Lys380, Lys611, and Lys628
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?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs)
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-
?
acetyl-CoA + [AcsA]-L-Lys
CoA + [AcsA]-N6-acetyl-L-Lys
AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs)
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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-
?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
-
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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r
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is AcCoA synthase, Nepsilon-lysine-acetylation
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is isocitrate lyase
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?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is AcCoA synthase, Nepsilon-lysine-acetylation
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-
?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
ACS is AcCoA synthase, Nepsilon-lysine-acetylation
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-
?
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
-
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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-
r
acetyl-CoA + [ACS]-L-Lys
CoA + [ACS]-N6-acetyl-L-Lys
-
ACS is Nepsilon-lysine-acetylated AcCoA synthase
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-
?
acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis
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acetyl-CoA + [BsAcsA]-L-Lys
CoA + [BsAcsA]-N6-acetyl-L-Lys
BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis
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acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
substrate is acetyl-CoA synthase Micau_0428. substrate mutant K619 is not acetylated
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acetyl-CoA + [Micau_0428]-L-Lys619
CoA + [Micau_0428]-N6-acetyl-L-Lys619
substrate is acetyl-CoA synthase Micau_0428. substrate mutant K619 is not acetylated
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acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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acetyl-CoA + [SeAcs]-L-Lys
CoA + [SeAcs]-N6-acetyl-L-Lys
SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs)
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additional information
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enzyme inactivates AMP-forming acyl-CoA synthases by acetylating the epsilon-amino group of a conserved, catalytic lysine residue. Substrate recognition motif is PK/RTXS/T/V/NGKX2K/R. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. No substrate: long-chain acyl-CoA synthase B
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additional information
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SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)
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additional information
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SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)
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additional information
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SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)
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evolution
enzyme BsAcsA is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. BsAcuA is a type-IV bGNAT enzyme
evolution
enzyme SaAcuA is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SaAcuA is a type-IV bGNAT enzyme
evolution
enzyme SePat is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SePat is a two-domain bGNAT that belongs to type I
evolution
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the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
evolution
-
enzyme BsAcsA is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. BsAcuA is a type-IV bGNAT enzyme
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evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
-
evolution
-
enzyme SePat is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SePat is a two-domain bGNAT that belongs to type I
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evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
-
evolution
-
enzyme SePat is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SePat is a two-domain bGNAT that belongs to type I
-
evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
-
evolution
-
enzyme SaAcuA is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SaAcuA is a type-IV bGNAT enzyme
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evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
-
evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
-
evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
-
evolution
-
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes
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metabolism
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enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
metabolism
-
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
metabolism
-
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
metabolism
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
metabolism
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
metabolism
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
metabolism
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes. The ACS gene and AcuABC operon are adjacent to each other, with AcuA functioning as the acetylase and AcuC as an NAD+-independent deacetylase
metabolism
inactive SaAcsAc is deacetylated (hence reactivated) by the NAD+-dependent (class III) sirtuin protein deacetylase (hereafter SaCobB). In vivo and in vitro evidence show that SaAcuA and SaCobB modulate the level of SaAcs activity in Staphylococcus aureus
metabolism
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enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes. The ACS gene and AcuABC operon are adjacent to each other, with AcuA functioning as the acetylase and AcuC as an NAD+-independent deacetylase
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metabolism
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enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
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metabolism
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enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
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metabolism
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inactive SaAcsAc is deacetylated (hence reactivated) by the NAD+-dependent (class III) sirtuin protein deacetylase (hereafter SaCobB). In vivo and in vitro evidence show that SaAcuA and SaCobB modulate the level of SaAcs activity in Staphylococcus aureus
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metabolism
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enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
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metabolism
-
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
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metabolism
-
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
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metabolism
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enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes
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physiological function
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enzyme PatA acetylates acetoacetyl-CoA synthase AacS at the active-site residue Lys617 and acetylation inactivates AacS. Acetylated AacS is deacetylated by a sirtuin-type protein deacetylase
physiological function
Gcn5-like protein acetyltransferase AcuA is the enzyme responsible for the acetylation of the AMP-forming acetyl coenzyme A synthetase AcsA. Acetylated AcsA is deacetylated by a sirtuin-type NAD+-dependent consuming deacetylase SrtN
physiological function
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protein acetyltransferase, Pat, catalyzes the acetylation at the apsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition
physiological function
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protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition
physiological function
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protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition
physiological function
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition
physiological function
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis
physiological function
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis
physiological function
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis. ACS activity is also post-translationally modified by GNAT protein acetyltransferase AcuA
physiological function
role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs
physiological function
role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs
physiological function
role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs. Acs from Staphylococcus aureus (SaAcs) activates acetate and weakly activates propionate, but does not activate organic acids longer than C3 or dicarboxylic acids (e.g. butyrate, malonate and succinate). SaAcs activity is regulated by AcuA (SaAcuA), a type-IV bGNAT. SaAcuA can acetylate or propionylate SaAcs reducing its activity by over 90% and 95% respectively. SaAcuA also succinylated SaAcs, but this is less effective in AcsA inhibition than acetylation or propionylation of AcsA. Malonyl-CoA leads to only a slight inhibition of AcsA activity
physiological function
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role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs
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physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis. ACS activity is also post-translationally modified by GNAT protein acetyltransferase AcuA
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physiological function
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role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs
-
physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis
-
physiological function
-
role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs
-
physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis
-
physiological function
-
enzyme PatA acetylates acetoacetyl-CoA synthase AacS at the active-site residue Lys617 and acetylation inactivates AacS. Acetylated AacS is deacetylated by a sirtuin-type protein deacetylase
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physiological function
-
role of lysine acylation in metabolism is the acetyl-coenzyme A synthetase (Acs) enzyme, overview. In prokaryotic and eukaryotic cells alike, Acs activity is downregulated by acetylation and reactivated by deacetylation. Proteins belonging to the bacterial GCN5-related N-acetyltransferase (bGNAT) superfamily acetylate the epsilon amino group of an active site lysine, inactivating Acs. Acs from Staphylococcus aureus (SaAcs) activates acetate and weakly activates propionate, but does not activate organic acids longer than C3 or dicarboxylic acids (e.g. butyrate, malonate and succinate). SaAcs activity is regulated by AcuA (SaAcuA), a type-IV bGNAT. SaAcuA can acetylate or propionylate SaAcs reducing its activity by over 90% and 95% respectively. SaAcuA also succinylated SaAcs, but this is less effective in AcsA inhibition than acetylation or propionylation of AcsA. Malonyl-CoA leads to only a slight inhibition of AcsA activity
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physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition
-
physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis
-
physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis
-
physiological function
-
protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition
-
physiological function
-
Gcn5-like protein acetyltransferase AcuA is the enzyme responsible for the acetylation of the AMP-forming acetyl coenzyme A synthetase AcsA. Acetylated AcsA is deacetylated by a sirtuin-type NAD+-dependent consuming deacetylase SrtN
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additional information
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key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity
additional information
key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity
additional information
-
key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity
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additional information
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key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity
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Tucker, A.C.; Escalante-Semerena, J.C.
Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans
Mol. Microbiol.
87
152-167
2013
Streptomyces lividans, Streptomyces lividans TK24
brenda
Crosby, H.A.; Escalante-Semerena, J.C.
The acetylation motif in AMP-forming Acyl coenzyme A synthases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris
J. Bacteriol.
196
1496-1504
2014
Rhodopseudomonas palustris
brenda
You, D.; Yao, L.L.; Huang, D.; Escalante-Semerena, J.C.; Ye, B.C.
Acetyl coenzyme A synthetase is acetylated on multiple lysine residues by a protein acetyltransferase with a single Gcn5-type N-acetyltransferase (GNAT) domain in Saccharopolyspora erythraea
J. Bacteriol.
196
3169-3178
2014
Saccharopolyspora erythraea (A4FK18), Saccharopolyspora erythraea DSM 40517 (A4FK18)
brenda
Liu, X.X; Liu, W.B.; Ye, B.C.
Regulation of a protein acetyltransferase in Myxococcus xanthus by the coenzyme NADP
J. Bacteriol.
198
623-632
2015
Myxococcus xanthus (Q1D7F7), Myxococcus xanthus
brenda
Xu, J.Y.; You, D.; Leng, P.Q.; Ye, B.C.
Allosteric regulation of a protein acetyltransferase in Micromonospora aurantiaca by the amino acids cysteine and arginine
J. Biol. Chem.
289
27034-27045
2014
Micromonospora aurantiaca (D9SZU3), Micromonospora aurantiaca, Micromonospora aurantiaca ATCC 27029 (D9SZU3), Micromonospora aurantiaca ATCC 27029
brenda
Jeffers, V.; Gao, H.; Checkley, L.A.; Liu, Y.; Ferdig, M.T.; Sullivan, W.J.
Garcinol inhibits GCN5-mediated lysine acetyltransferase activity and prevents replication of the parasite Toxoplasma gondii
Antimicrob. Agents Chemother.
60
2164-2170
2016
Staphylococcus aureus (A0A0D3Q886), Bacillus subtilis (P39065), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZMX2), Bacillus subtilis 168 (P39065), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (Q8ZMX2), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZMX2), Staphylococcus aureus HG001 (A0A0D3Q886)
brenda
Favrot, L.; Blanchard, J.; Vergnolle, O.
Bacterial GCN5-related N-acetyltransferases from resistance to regulation
Biochemistry
55
989-1002
2016
Rhodopseudomonas palustris, Streptomyces coelicolor, Streptomyces lividans, Mycolicibacterium smegmatis (A0R3F9), Mycobacterium tuberculosis (O05581), Bacillus subtilis (P39065), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZMX2), Bacillus subtilis 168 (P39065), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (Q8ZMX2), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZMX2), Mycolicibacterium smegmatis ATCC 700084 (A0R3F9), Mycobacterium tuberculosis H37Rv (O05581), Mycobacterium tuberculosis ATCC 25618 (O05581), Mycolicibacterium smegmatis mc(2)155 (A0R3F9)
brenda