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- W31751639 abstract "Lysine (K) acetylation refers to transfer of the acetyl moiety from acetyl-CoA to the ε-amino group of a lysine residue. This is posttranslational and reversible, with its level dynamically maintained by lysine acetyltransferases (KATs) and deacetylases (KDACs). Traditionally, eukaryotic KDACs have been referred to as HDACs (histone deacetylases). Recent proteomic studies have revealed that hundreds of bacterial proteins and thousands of eukaryotic proteins contain acetyl-lysine (AcK) residues, indicating that K-acetylomes are comparable to phosphoproteomes. The current challenges are to assign enzymes that execute specific acetylation events, to determine the impact of these events, and to relate this modification to other posttranslational modifications, cell signaling networks, and pathophysiology under different cellular and developmental contexts. In this chapter, we provide a brief overview about the acetylomes, KATs, HDACs, AcK-recognizing protein domains, and acetylation-modulating therapeutics, and emphasize the latest developments in related areas. The remaining chapters of the book focus on and cover various aspects of HDACs (both the Rpd3/Hda1 and sirtuin families), which shall provide novel insights into how to utilize these enzymes for developing a new generation of HDAC-related therapeutics." @default.
- W31751639 created "2016-06-24" @default.
- W31751639 creator A5004904475 @default.
- W31751639 creator A5046514658 @default.
- W31751639 creator A5054244512 @default.
- W31751639 date "2011-01-01" @default.
- W31751639 modified "2023-10-08" @default.
- W31751639 title "K-Acetylation and Its Enzymes: Overview and New Developments" @default.
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- W31751639 doi "https://doi.org/10.1007/978-3-642-21631-2_1" @default.
- W31751639 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21879443" @default.
- W31751639 hasPublicationYear "2011" @default.
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