A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
STRUCTURE BY NMR OF 715-832, AND MUTAGENESIS OF VAL-752; TYR-760; TYR-802 AND TYR-809.
Structure and ligand of a histone acetyltransferase bromodomain
Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases.
Kinetic mechanism of human histone acetyltransferase P/CAF
p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
Acetylation of histones and transcription-related factors.
The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc.
Matching the transcription machinery to the right DNA
Structure and function of histone acetyltransferases
Acetylation by histone acetyltransferase CREB-binding protein/p300 of STAT6 is required for transcriptional activation of the 15-lipoxygenase-1 gene
Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
Structure of histone acetyltransferases.
Bromodomain: an acetyl-lysine binding domain.
Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain.
Insights into structure and function of GCN5/PCAF and yEsa 1 histone acetyltransferase domains:.
Biochemical and structural characterization of recombinant histone acetyltransferase proteins.
Use of nuclear magnetic resonance spectroscopy to study structure-function of bromodomains.
According to the literature [2], the catalytic mechanism is similar to that of histone acetyltransferase type B (T00034 in EzCatDB). The reaction proceeds via a direct nucleophilic attack of the substrate histone lysine on the carbonyl carbon of acyl group of acetyl-CoA (see [2]). Hydrophobic residues (Phe563, Phe568, Ile571, Val572, Leu606, Ile637 & Tyr640) raise the pKa of the general base, Glu570. The mainchain amide of Cys574 stabilizes the tetrahedral intermediate.