Sandbox Reserved 1546: Difference between revisions

==Relevance==

It is known that the 5h86 Human Gcn5 enzyme functions as an acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. The experiment was tested on Gcn5 (Gcn5L2), more specifically the lysine acetylation of this enzyme <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. This is important to understand because the acyltransferase activity of the Gcn5L2 becomes much weaker with increasing acyl chain length <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. The researchers were inspired by previous studies that identified a chemically diverse array of lysine acyl modification in vivo, and more specifically - the acyl chain of acetyltransferase specificity in the human Gcn5 <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. In short, they want to experiment and test which acyl-chain donor had the highest enzymatic activity and to characterize the specificity of the acyl-chain of the human Gcn5, which catalyzes the acetylation of histone peptides much quicker than other methods like propionylation or butyrylation <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. Through the experiment, it was found that via this method, the active sites of Gcn5 can accommodate longer acyl chains without many structural rearrangements <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>.

== References ==

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