Cloned (Comment) | Organism |
---|---|
expression of monofluorinated phenylalanine analogues, incorporated into tGCN5, using a phenylalanine auxotrophic Escherichia coli strain AFIQ containing the plasmid IQ, which constitutively expresses the lacIq repressor. Determination of Phe replacement by MALDI-TOF mass spectrometry | Tetrahymena thermophila |
Protein Variants | Comment | Organism |
---|---|---|
additional information | recombinant enzyme containing fluorinated Phe analogues shows reduced half-life: 27.5 min for the recombinant p-fluorophenylalanine-substituted tGCN5, 5.4 min for recombinant m-fluorophenylalanine-substituted tGCN5, and 6.8 min for recombinant o-fluorophenylalanine-substituted tGCN5 | Tetrahymena thermophila |
General Stability | Organism |
---|---|
the recombinant wild-type tGCN5 shows a half-life of 31.2 min | Tetrahymena thermophila |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | effects of three monofluorinated phenylalanine analogs p-fluorophenylalanine, m-fluorophenylalanine, and o-fluorophenylalanine on the stability and enzymatic activity of tGCN5, overview | Tetrahymena thermophila |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.69 | - |
histone H3 | recombinant p-fluorophenylalanine-substituted tGCN5 | Tetrahymena thermophila | |
0.8 | - |
histone H3 | recombinant o-fluorophenylalanine-substituted wild-type tGCN5 | Tetrahymena thermophila | |
1.05 | - |
histone H3 | recombinant wild-type tGCN5 | Tetrahymena thermophila | |
2.09 | - |
histone H3 | recombinant m-fluorophenylalanine-substituted wild-type tGCN5 | Tetrahymena thermophila |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + histone H3 | Tetrahymena thermophila | acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK | CoA + acetylhistone H3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Tetrahymena thermophila | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + histone H3 | acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK | Tetrahymena thermophila | CoA + acetylhistone H3 | - |
? | |
acetyl-CoA + histone H3 | acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK. Phe125 and Phe164 interact with the substrate, but are not directly involved in the acetylation reaction, while residues Glu122, Val123 and Tyr160 are critical for catalysis | Tetrahymena thermophila | CoA + acetylhistone H3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | tGCN5 is comprised of five alpha-helices and six beta-strands, with N-terminal and C-terminal regions separated by a deep hydrophobic cleft, structure, overview. Phe125 and Phe164 interact with the substrate, but are not directly involved in the acetylation reaction, while residues Glu122, Val123 and Tyr160 are critical for catalysis | Tetrahymena thermophila |
Synonyms | Comment | Organism |
---|---|---|
HAT | - |
Tetrahymena thermophila |
tGCN5 | - |
Tetrahymena thermophila |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Tetrahymena thermophila |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.053 | - |
histone H3 | recombinant o-fluorophenylalanine-substituted tGCN5 | Tetrahymena thermophila | |
0.14 | - |
histone H3 | recombinant p-fluorophenylalanine-substituted tGCN5 | Tetrahymena thermophila | |
0.25 | - |
histone H3 | recombinant m-fluorophenylalanine-substituted tGCN5 | Tetrahymena thermophila | |
0.87 | - |
histone H3 | recombinant wild-type tGCN5 | Tetrahymena thermophila |