Department of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53706, USA.
Chembiochem. 2011 Jan 24;12(2):290-8. doi: 10.1002/cbic.201000438. Epub 2010 Nov 24.
Post-translational modifications of histones elicit structural and functional changes within chromatin that regulate various epigenetic processes. Epigenetic mechanisms rely on enzymes whose activities are driven by coenzymes and metabolites from intermediary metabolism. Lysine acetyltransferases (KATs) catalyze the transfer of acetyl groups from acetyl-CoA to epsilon amino groups. Utilization of this critical metabolite suggests these enzymes are modulated by the metabolic status of the cell. This review highlights studies linking KATs to metabolism. We cover newly identified acyl modifications (propionylation and butyrylation), discuss the control of KAT activity by cellular acetyl-CoA levels, and provide insights into how acetylation regulates metabolic proteins. We conclude with a discussion of the current approaches to identifying novel KATs and their metabolic substrates.
组蛋白的翻译后修饰引发染色质内的结构和功能变化，调节各种表观遗传过程。表观遗传机制依赖于酶，其活性由辅酶和中间代谢产物驱动。赖氨酸乙酰转移酶 (KAT) 催化乙酰辅酶 A 上的乙酰基转移到 ε 氨基上。这种关键代谢物的利用表明这些酶受到细胞代谢状态的调节。本综述强调了将 KAT 与代谢联系起来的研究。我们涵盖了新发现的酰基修饰（丙酰化和丁酰化），讨论了细胞乙酰辅酶 A 水平对 KAT 活性的控制，并深入了解乙酰化如何调节代谢蛋白。最后，我们讨论了目前鉴定新的 KAT 和其代谢底物的方法。
