Sandbox Reserved 1546: Difference between revisions
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Makayla Yang (talk | contribs) No edit summary |
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<p>[[Image:Thiolase_reaction.PNG|400px|center]]</p> | <p>[[Image:Thiolase_reaction.PNG|400px|center]]</p> | ||
<p><center>'''Figure 1''': Reaction mechanism of Acetoacetyl-CoA to two Acetyl-CoAs with the enzyme thiolase. Image obtained from class powerpoints.</center></p> | <p><center>'''Figure 1''': Reaction mechanism of Acetoacetyl-CoA to two Acetyl-CoAs with the enzyme thiolase. Image obtained from class powerpoints.</center></p> | ||
<p>The specific acetyltransferase we are particularly interested in is known as 5H86 which is a Human Gcn5 bound to butyryl-CoA <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. Gcn5 is a conserved acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. To better understand how 5H86 is related to fatty acid degradation, we have to understand how they operate as a histone acetyltransferase (HATs). HATs are enzymes that acetylate conserved lysine amino acids on histone proteins <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. This occurs by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. When DNA is wrapped around histones, an acetyl group is transferred to the histones, allowing genes to be turned on and off <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>. In conclusion, histone acetylation contribute to the increase of gene expression <ref name = "Structural basis for acyl-group discrimination by human Gcn5L2"/>.</p> | |||
<p>hi</p> | |||
