期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 4, 页码 1149-1152出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201408763
关键词
click chemistry; fatty acids; peptides; photochemistry; protein modifications
资金
- Hong Kong Research Grants Council, Early Career Scheme [HKU 709813P]
- University of Hong Kong [201211159017]
Acylation of proteins with fatty acids is important for the regulation of membrane association, trafficking, subcellular localization, and activity of many cellular proteins. While significant progress has been made in our understanding of the two major forms of protein acylation with fatty acids, N-myristoylation and S-palmitoylation, studies of the acylation of lysine residues, within proteins, with fatty acids have lagged behind. Demonstrated here is the use of integrative chemical biology approaches to examine human sirtuins as de-fatty-acid acylases invitro and in cells. Photo-crosslinking chemistry is used to investigate enzymes which recognize fatty-acid acylated lysine. Human Sirt2 was identified as a robust lysine de-fatty-acid acylase invitro. The results also show that Sirt2 can regulate the acylation of lysine residues, of proteins, with fatty acids within cells.
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