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Literature summary for 2.3.1.B34 extracted from

  • 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 (2016), Antimicrob. Agents Chemother., 60, 2164-2170 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [AcsA]-L-Lys Staphylococcus aureus AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) CoA + [AcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [AcsA]-L-Lys Staphylococcus aureus HG001 AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) CoA + [AcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [BsAcsA]-L-Lys Bacillus subtilis BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis CoA + [BsAcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [BsAcsA]-L-Lys Bacillus subtilis 168 BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis CoA + [BsAcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys Salmonella enterica subsp. enterica serovar Typhimurium SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) CoA + [SeAcs]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) CoA + [SeAcs]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) CoA + [SeAcs]-N6-acetyl-L-Lys
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?
propionyl-CoA + [AcsA]-L-Lys Staphylococcus aureus AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) CoA + [AcsA]-N6-propionyl-L-Lys
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?
succinyl-CoA + [AcsA]-L-Lys Staphylococcus aureus AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs). AcuA is the first documented case of a bacterial GNAT capable of succinylation CoA + [AcsA]-N6-succinyl-L-Lys
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?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P39065
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Bacillus subtilis 168 P39065
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Salmonella enterica subsp. enterica serovar Typhimurium Q8ZMX2
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Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 Q8ZMX2
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Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 Q8ZMX2
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Staphylococcus aureus A0A0D3Q886
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Staphylococcus aureus HG001 A0A0D3Q886
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [AcsA]-L-Lys AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) Staphylococcus aureus CoA + [AcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [AcsA]-L-Lys AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs), lysine residue K546 is acetylated Staphylococcus aureus CoA + [AcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [AcsA]-L-Lys AcsA is the AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) Staphylococcus aureus HG001 CoA + [AcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [AcsA]-L-Lys AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs), lysine residue K546 is acetylated Staphylococcus aureus HG001 CoA + [AcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [AcsA]-L-Lys SaAcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus, lysine residue K546 is acetylated Bacillus subtilis CoA + [SaAcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [AcsA]-L-Lys SaAcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus, lysine residue K546 is acetylated Bacillus subtilis 168 CoA + [SaAcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [BsAcsA]-L-Lys BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis Bacillus subtilis CoA + [BsAcsA]-N6-acetyl-L-Lys
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?
acetyl-CoA + [BsAcsA]-L-Lys BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis(BsAcsA) Staphylococcus aureus CoA + [BsAcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [BsAcsA]-L-Lys BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis Bacillus subtilis 168 CoA + [BsAcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [BsAcsA]-L-Lys BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis(BsAcsA) Staphylococcus aureus HG001 CoA + [BsAcsA]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) Staphylococcus aureus CoA + [SeAcs]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) Salmonella enterica subsp. enterica serovar Typhimurium CoA + [SeAcs]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is AMP-forming acetyl-CoA synthetase from Salmonella enterica Bacillus subtilis CoA + [SeAcs]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is AMP-forming acetyl-CoA synthetase from Salmonella enterica Bacillus subtilis 168 CoA + [SeAcs]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 CoA + [SeAcs]-N6-acetyl-L-Lys
-
?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 CoA + [SeAcs]-N6-acetyl-L-Lys
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?
acetyl-CoA + [SeAcs]-L-Lys SeAcs is the AMP-forming acetyl-CoA synthetase from Salmonella enterica (SeAcs) Staphylococcus aureus HG001 CoA + [SeAcs]-N6-acetyl-L-Lys
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?
additional information enzyme BsAcuA acetylates BsAcsA and also SaAcsA from Staphylococcus aureus, as well as SeAcs from Salmonella enterica Bacillus subtilis ?
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additional information enzyme SePat acetylates SeAcs, but it fails to acetylate AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) and Bacillus subtilis (BsAcsA) Salmonella enterica subsp. enterica serovar Typhimurium ?
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additional information 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 Staphylococcus aureus ?
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additional information enzyme BsAcuA acetylates BsAcsA and also SaAcsA from Staphylococcus aureus, as well as SeAcs from Salmonella enterica Bacillus subtilis 168 ?
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additional information enzyme SePat acetylates SeAcs, but it fails to acetylate AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) and Bacillus subtilis (BsAcsA) Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 ?
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additional information enzyme SePat acetylates SeAcs, but it fails to acetylate AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) and Bacillus subtilis (BsAcsA) Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 ?
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additional information 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 Staphylococcus aureus HG001 ?
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propionyl-CoA + [AcsA]-L-Lys AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) Staphylococcus aureus CoA + [AcsA]-N6-propionyl-L-Lys
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?
propionyl-CoA + [AcsA]-L-Lys AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs), lysine residue K546 is propionylated Staphylococcus aureus CoA + [AcsA]-N6-propionyl-L-Lys
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?
succinyl-CoA + [AcsA]-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 Staphylococcus aureus CoA + [AcsA]-N6-succinyl-L-Lys
-
?
succinyl-CoA + [AcsA]-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 Staphylococcus aureus CoA + [AcsA]-N6-succinyl-L-Lys
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?

Synonyms

Synonyms Comment Organism
acetoin utilization protein UniProt Staphylococcus aureus
acetoin utilization protein UniProt Bacillus subtilis
AcuA
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Staphylococcus aureus
AcuA
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Bacillus subtilis
BsAcuA
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Bacillus subtilis
Pat
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Salmonella enterica subsp. enterica serovar Typhimurium
peptidyl-lysine N-acetyltransferase UniProt Salmonella enterica subsp. enterica serovar Typhimurium
SaAcuA
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Staphylococcus aureus
SePat
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Salmonella enterica subsp. enterica serovar Typhimurium
type-I bGNAT
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Salmonella enterica subsp. enterica serovar Typhimurium
type-IV bGNAT
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Staphylococcus aureus
type-IV bGNAT
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Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
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Staphylococcus aureus
acetyl-CoA
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Salmonella enterica subsp. enterica serovar Typhimurium
acetyl-CoA
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Bacillus subtilis
propionyl-CoA
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Staphylococcus aureus
succinyl-CoA
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Staphylococcus aureus

General Information

General Information Comment Organism
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 Bacillus subtilis
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 Staphylococcus aureus
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 Salmonella enterica subsp. enterica serovar Typhimurium
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 Staphylococcus aureus
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 Salmonella enterica subsp. enterica serovar Typhimurium
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 Bacillus subtilis
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 Staphylococcus aureus