The Acyl-CoA Specificity of Human Lysine Acetyltransferase KAT2A
| Autor: | Ananya Anmangandla, Yuxiang Ren, Qin Fu, Sheng Zhang, Hening Lin |
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| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Biochemistry, 61 (17) |
| ISSN: | 0006-2960 1520-4995 |
| DOI: | 10.3929/ethz-b-000569868 |
| Popis: | Protein post-translational modification sserve to regulate a broad range of cellular functions including signal transduction, transcription, and metabolism. Protein lysine residue sundergo many post-translational acylations and are regulated by a range of enzymes, such as histone acetyl transferases (HATs)and histone deacetylases (HDACs).KAT2A,well characterized as a lysine acetyltransferase for both histone and nonhistone substrates, has been reported to tolerate addition alacyl-CoA substrates, such as succinyl-CoA, and shows nonacetyl transferase activity in specific biologicalcontexts.In thiswork, we investigatethe acyl-CoA substrate preference of KAT2A and attempt to determine whether and to what extent addition alacyl-CoA substrates may be utilized by KAT2A in a cellula rcontext. We show that while KAT2A can bind and utilize malonyl-CoA, its activity with succinyl-CoA or glutaryl-CoA is very weak, and acetylation is still the most efficient activity for KAT2A in vitro and in cells. Biochemistry, 61 (17) ISSN:0006-2960 ISSN:1520-4995 |
| Databáze: | OpenAIRE |
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