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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.48 gene GCN5, quantitative RT-PCR enzyme expression analysis, recombinant ectopical expression of HA-tagged enzyme TgGCN5b Toxoplasma gondii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.48 garcinol isolated from Garcinia indica, inhibits GCN5-mediated lysine acetyltransferase activity and prevents the replication of the parasite. Treatment of tachyzoites with garcinol leads to a reduction of global lysine acetylation, particularly on histone H3 and TgGCN5b itself. transcriptome sequencing (RNA-seq), which reveals increasing aberrant gene expression coincident with increasing concentrations of garcinol. The majority of the genes that are most significantly affected by garcinol are also associated with TgGCN5b in a previously reported chromatin immunoprecipitation assay with microarray technology analysis. The dysregulated gene expression induced by garcinol significantly inhibits Toxoplasma tachyzoite replication, and the concentrations used exhibit no overt toxicity on human host cells. Garcinol also reduces autoacetylation of TgGCN5b, garcinol treatment results in a 65% reduction in the acetylation level of HA-tagged TgGCN5b. Garcinol-mediated changes in the parasite transcriptome, overview Toxoplasma gondii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.48 nucleus
-
 Toxoplasma gondii 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 acetyl-CoA + [BsAcsA]-L-Lys Bacillus subtilis BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis CoA + [BsAcsA]-N6-acetyl-L-Lys
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 propionyl-CoA + [AcsA]-L-Lys Staphylococcus aureus AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) CoA + [AcsA]-N6-propionyl-L-Lys
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.48 acetyl-CoA + [histone H3]-L-lysine9 Toxoplasma gondii
-
 CoA + [histone H3]-N6-acetyl-L-lysine9
-
 ?
2.3.1.48 acetyl-CoA + [protein]-L-lysine Toxoplasma gondii
-
 CoA + [protein]-N6-acetyl-L-lysine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.B34 Bacillus subtilis P39065
-
-
2.3.1.B34 Bacillus subtilis 168 P39065
-
-
2.3.1.B34 Salmonella enterica subsp. enterica serovar Typhimurium Q8ZMX2
-
-
2.3.1.B34 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 Q8ZMX2
-
-
2.3.1.B34 Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 Q8ZMX2
-
-
2.3.1.B34 Staphylococcus aureus A0A0D3Q886
-
-
2.3.1.B34 Staphylococcus aureus HG001 A0A0D3Q886
-
-
2.3.1.48 Toxoplasma gondii Q9NIS0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.48 wild-type and recombinant HA-tagged enzyme Toxoplasma gondii

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.48 tachyzoite
-
 Toxoplasma gondii
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 acetyl-CoA + [BsAcsA]-L-Lys BsAcsA is the AMP-forming acetyl-CoA synthetase from Bacillus subtilis Bacillus subtilis CoA + [BsAcsA]-N6-acetyl-L-Lys
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 acetyl-CoA + [SeAcs]-L-Lys SeAcs is AMP-forming acetyl-CoA synthetase from Salmonella enterica Bacillus subtilis CoA + [SeAcs]-N6-acetyl-L-Lys
-
 ?
2.3.1.B34 acetyl-CoA + [SeAcs]-L-Lys SeAcs is AMP-forming acetyl-CoA synthetase from Salmonella enterica Bacillus subtilis 168 CoA + [SeAcs]-N6-acetyl-L-Lys
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 additional information enzyme BsAcuA acetylates BsAcsA and also SaAcsA from Staphylococcus aureus, as well as SeAcs from Salmonella enterica Bacillus subtilis ?
-
-
2.3.1.B34 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 ?
-
-
2.3.1.B34 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 ?
-
-
2.3.1.B34 additional information enzyme BsAcuA acetylates BsAcsA and also SaAcsA from Staphylococcus aureus, as well as SeAcs from Salmonella enterica Bacillus subtilis 168 ?
-
-
2.3.1.B34 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 ?
-
-
2.3.1.B34 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 ?
-
-
2.3.1.B34 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 ?
-
-
2.3.1.B34 propionyl-CoA + [AcsA]-L-Lys AcsA is AMP-forming acetyl-CoA synthetase from Staphylococcus aureus (SaAcs) Staphylococcus aureus CoA + [AcsA]-N6-propionyl-L-Lys
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.B34 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
-
 ?
2.3.1.48 acetyl-CoA + [histone H3]-L-lysine9
-
 Toxoplasma gondii CoA + [histone H3]-N6-acetyl-L-lysine9
-
 ?
2.3.1.48 acetyl-CoA + [protein]-L-lysine
-
 Toxoplasma gondii CoA + [protein]-N6-acetyl-L-lysine
-
 ?
2.3.1.48 additional information TgGCN5b performs autoacetylation. Proteome-wide acetylome analyses of Toxoplasma tachyzoites identifies seven acetylated lysines on TgGCN5b, i.e. K811, K857, K941, K989, K997, K1002, and K1027 Toxoplasma gondii ?
-
-

Synonyms

EC Number Synonyms Comment Organism
2.3.1.B34 acetoin utilization protein UniProt Staphylococcus aureus
2.3.1.B34 acetoin utilization protein UniProt Bacillus subtilis
2.3.1.B34 AcuA
-
 Staphylococcus aureus
2.3.1.B34 AcuA
-
 Bacillus subtilis
2.3.1.B34 BsAcuA
-
 Bacillus subtilis
2.3.1.B34 Pat
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34 peptidyl-lysine N-acetyltransferase UniProt Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34 SaAcuA
-
 Staphylococcus aureus
2.3.1.B34 SePat
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34 type-I bGNAT
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34 type-IV bGNAT
-
 Staphylococcus aureus
2.3.1.B34 type-IV bGNAT
-
 Bacillus subtilis
2.3.1.48 GCN5 family KAT
-
 Toxoplasma gondii
2.3.1.48 GCN5 lysine acetyltransferase
-
 Toxoplasma gondii
2.3.1.48 TgGCN5b
-
 Toxoplasma gondii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.48 37
-
 assay at Toxoplasma gondii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.48 8
-
 assay at Toxoplasma gondii

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.B34 acetyl-CoA
-
 Staphylococcus aureus
2.3.1.B34 acetyl-CoA
-
 Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34 acetyl-CoA
-
 Bacillus subtilis
2.3.1.B34 propionyl-CoA
-
 Staphylococcus aureus
2.3.1.B34 succinyl-CoA
-
 Staphylococcus aureus
2.3.1.48 acetyl-CoA
-
 Toxoplasma gondii

General Information

EC Number General Information Comment Organism
2.3.1.B34 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
2.3.1.B34 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
2.3.1.B34 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
2.3.1.B34 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
2.3.1.B34 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
2.3.1.B34 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
2.3.1.B34 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
2.3.1.48 physiological function enzyme TgGCN5b is the only nuclear GCN5 family KAT known to be required for Toxoplasma tachyzoite replication Toxoplasma gondii