2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	A group of enzymes with differing specificities towards histone acceptors	-	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	acetylation of lysine 5, 8, 12, and 16 of free histone H4	487086, 487090, 487093	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	binding motifs	-, 487102	
2.3.1.48	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	703350	
2.3.1.48	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	703350	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	enzymes are also active as transcription coactivators and corepressors of transcription factors in gene regulation, acetylation of transcription factors, overview	-, 487089	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	mechanisms	-, 487089, 487090, 487102	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	MORF protein is also active as transcription factor	487090	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	non-processive mechanism, where the NuA4 histone acetyltransferasecomplex dissociates from substrate after each acetylation event	718912	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	ordered sequential catalytic mechanism of the MYST HAT with a direct-attack mechanism and direct acetyl transfer mechanism, not mediated by Cys304, within an Esa1‚acetyl-CoA‚histone ternary complex, acetyl-CoA binds first and CoA is the last product released	672263	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	PCAF and Gcn5 protein, fully ordered Bi-Bi kinetic mechanism with acetyl-CoA binding before histone H3	487095, 487096, 487097	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	ping-pong catalytic mechanism of bi-substrate histone acetyltransferase KAT8	736051	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	ping-pong mechanism	487074	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	ping-pong mechanism, enzyme form NII	487069	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	rapid equilibrium ordered bireactant mechanism	487072	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	sequential mechanism in which acetyl-CoA and H3 bind to a complex of isoform Rtt109 and histone chaperone Vps75 without obligate order, followed by the direct attack of the unprotonated epsilon-amino group on acetyl-CoA, transferring the acetyl-group to H3 lysine residues The chemical attack of substrate lysine on the bound acetyl-CoA is the rate-limiting step of catalysis	718878	
2.3.1.48	acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine	ternary complexed mechanism for PCAF and Gnc5	487096, 487097