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Literature summary for 2.3.1.48 extracted from
- Catalysis and substrate selection by histone/protein lysine acetyltransferases (2008), Curr. Opin. Struct. Biol., 18, 682-689.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | HATs form multisubunit complexes, and HAT interacting partners appear to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | Homo sapiens | |
| additional information | protein factors such as E1A and Nap1 can modulate p300/CBP HAT activity. Rtt109 requires a histone chaperone for efficient catalysis. HATs form multisubunit complexes, and HAT interacting partners appear to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | Saccharomyces cerevisiae | |
| Vps75/Asf1 | helper proteins required by Rtt109 for full catalytic activity. Stimulation of Rtt109 activity by Vps75 results in 50fold increase of the kcat value with unaltered Km | Saccharomyces cerevisiae | |
| Yng2/Epl1 | helper proteins required by Esa1 for full catalytic activity. Esa1 minimally requires Yng2 and Epl1 for full catalytic activity and nucleosome recognition | Saccharomyces cerevisiae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystallization of the catalytic domains of Gcn5 and p/CAF with a number of peptide substrates including sequences from histone and p53 | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | protein factors such as E1A and Nap1 can modulate p300/CBP HAT activity | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| nucleus | - |
Homo sapiens | 5634 | - |
| nucleus | - |
Saccharomyces cerevisiae | 5634 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + histone H3 | Homo sapiens | - |
CoA + acetylhistone H3 | - |
? |  |
| acetyl-CoA + histone H3 | Tetrahymena sp. | - |
CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | Saccharomyces cerevisiae | Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56 | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | Tetrahymena sp. GCN5 | - |
CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H4 | Homo sapiens | - |
CoA + acetylhistone H4 | - |
? | |
| additional information | Saccharomyces cerevisiae | HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | ? | - |
? | |
| additional information | Homo sapiens | in response to DNA damage, Tip60 acetylates ATM, a DNA damage related kinase, allowing for phosphorylation of Chk2 and p53 by ATM. HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
Tip60, p/CAF, and p300 | - |
| Saccharomyces cerevisiae | - |
p300, Gcn5, Rtt109, and Esa1 | - |
| Tetrahymena sp. | - |
GCN5 | - |
| Tetrahymena sp. GCN5 | - |
GCN5 | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine | conserved catalytic mechanisms of HATs, overview. p300 utilizes a special type of sequential mechanism with a short-lived ternary complex, known as a Theorell-Chance mechanism | Homo sapiens | |
| acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine | conserved catalytic mechanisms of HATs, overview. p300 utilizes a special type of sequential mechanism with a short-lived ternary complex, known as a Theorell-Chance mechanism. For Gcn5, p/CAF, and p300, only 3 to 5 residues on either side of the substrate lysine are required for efficient binding and catalysis by the catalytic domain | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + histone H3 | - |
Homo sapiens | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | - |
Tetrahymena sp. | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56 | Saccharomyces cerevisiae | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56. The sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved with other GNAT members | Saccharomyces cerevisiae | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | the sequence G-K-X-P within histone H3 makes several key contacts within the active site that are conserved in GNAT members including p/CAF | Homo sapiens | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | the sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved in GNAT members | Tetrahymena sp. | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | - |
Tetrahymena sp. GCN5 | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H3 | the sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved in GNAT members | Tetrahymena sp. GCN5 | CoA + acetylhistone H3 | - |
? | |
| acetyl-CoA + histone H4 | - |
Homo sapiens | CoA + acetylhistone H4 | - |
? | |
| acetyl-CoA + histone H4 | full-length histone H4 is acetylated 2000fold faster than histone tail peptides | Saccharomyces cerevisiae | CoA + acetylhistone H4 | - |
? | |
| additional information | HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | in response to DNA damage, Tip60 acetylates ATM, a DNA damage related kinase, allowing for phosphorylation of Chk2 and p53 by ATM. HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | Homo sapiens | ? | - |
? | |
| additional information | Gcn5 and p300 appear to be constituitive HATs that do not require helper proteins to exhibit full catalytic activity. Esa1 and Rtt109 represent low-activity HATs that are stimulated by regulatory helper proteins, Yng2-Epl1 and Vps75/Asf1, respectively. p300/CBP exhibits the broadest protein specificity, p300 prefers histone acetylation sites with a positive charge in the -3 or +4 position. Ability of some HATs to utilize longer chain acyl-CoA, i.e. propionyl-CoA | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | Gcn5 appears to be constituitive HAT that does not require helper proteins to exhibit full catalytic activity | Tetrahymena sp. | ? | - |
? | |
| additional information | p/CAF and p300 appear to be constitutive HATs that do not require helper proteins to exhibit full catalytic activity | Homo sapiens | ? | - |
? | |
| additional information | Gcn5 appears to be constituitive HAT that does not require helper proteins to exhibit full catalytic activity | Tetrahymena sp. GCN5 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | ability of HATs to form distinct multi-subunit complexes. The human NuA4 complex contains Tip60, but also ATM, a DNA damage related kinase. HAT interacting partners appear to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex | Homo sapiens |
| More | ability of HATs to form distinct multi-subunit complexes. The SAGA complex contains the histone ubiquitin protease Ubp8 and the histone acetyltransferase Gcn5 | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Esa1 | - |
Saccharomyces cerevisiae |
| Gcn5 | - |
Saccharomyces cerevisiae |
| Gcn5 | - |
Tetrahymena sp. |
| HAT | - |
Saccharomyces cerevisiae |
| HAT | - |
Tetrahymena sp. |
| histone/protein lysine acetyltransferase | - |
Saccharomyces cerevisiae |
| KAT11 | - |
Saccharomyces cerevisiae |
| KAT2 | - |
Saccharomyces cerevisiae |
| KAT5 | - |
Saccharomyces cerevisiae |
| More | Esa1 and MOZ belong to the MYST family of histone acetyltransferases | Saccharomyces cerevisiae |
| p/CAF | - |
Homo sapiens |
| p300 | - |
Homo sapiens |
| p300 | - |
Saccharomyces cerevisiae |
| Rtt109 | - |
Saccharomyces cerevisiae |
| Tip60 | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Tetrahymena sp. | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the SAGA complex contains the histone ubiquitin protease Ubp8 and the histone acetyltransferase Gcn5 and is responsible for efficient transcription of SAGA regulated genes such as GAL1 and ADH2 | Saccharomyces cerevisiae |
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