2.3.1.B34: [protein]-L-lysine N-acetyltransferase
This is an abbreviated version!
For detailed information about [protein]-L-lysine N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.B34
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2.3.1.B34
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deacetylase
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deacetylation
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typhimurium
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gcn5-related
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nad+-dependent
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archaeon
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mycobacteria
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synthetases
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hild
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histone
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sulfolobus
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enterica
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camp
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tuberculosis
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serovar
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smegmatis
- 2.3.1.B34
- deacetylase
-
deacetylation
- typhimurium
-
gcn5-related
-
nad+-dependent
- archaeon
- mycobacteria
- synthetases
- hild
- histone
-
sulfolobus
-
enterica
- camp
- tuberculosis
-
serovar
- smegmatis
Reaction
Synonyms
acetoin utilization protein, acetyltransferase Pat, AcuA, ArtC, BsAcuA, epsilonN-lysine acetyltransferase, GCN5-related N-acetyltransferase, KAT, Micau_1670, MSMEG_5458, Mxan_3215, Pat, PatA, peptidyl-lysine N-acetyltransferase, protein acetyltransferase, Rv0998, SaAcuA, SACE_5148, SePat, SSPG_01886, type-I bGNAT, type-IV bGNAT, YhiQ
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General Information
General Information on EC 2.3.1.B34 - [protein]-L-lysine N-acetyltransferase
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evolution
metabolism
physiological function
additional information
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
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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
-
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
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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
-
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 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
-
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
-
-
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
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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. 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
-
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
-
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
-
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
-
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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
-
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
-
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. 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
-
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
-
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
-
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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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
-
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
-