| 货号 | 17848S |
| 供应商 | CST |
| 背景 | Lysine is subject to a wide array of regulatory post-translational modifications due to its positively charged ε-amino group side chain. The most prevalent of these are ubiquitination and acetylation, which are highly conserved among prokaryotes and eukaryotes (1,2). Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize lysine’s positive charge and confer structural alterations affecting substrate protein function. Lysine acetylation is catalyzed by histone acetyltransferases, HATs, using acetyl-CoA as a cofactor (3,4). Deacylation is mediated by histone deacetylases, HDACs 1-11, and NAD-dependent Sirtuins 1-7. Some sirtuins have little to no deacetylase activity, suggesting that they are better suited for other acyl lysine substrates (5). |
| 存放说明 | -20C |
| 参考文献 | Liu, Z. et al. (2014) Nucleic Acids Res 42, D531-6. Lee, S. (2013) Toxicol Res 29, 81-6. Lin, H. et al. (2012) ACS Chem Biol 7, 947-60. Zhang, Z. et al. (2011) Nat Chem Biol 7, 58-63. Du, J. et al. (2011) Science 334, 806-9. Chen, Y. et al. (2007) Mol Cell Proteomics 6, 812-9. Cheng, Z. et al. (2009) Mol Cell Proteomics 8, 45-52. Newman, J.C. et al. (2012) J Biol Chem 287, 42436-43. |
The Motif Logo was generated from a PTMScan® LC-MS/MS experiment using 430 nonredundant tryptic peptides derived from mouse liver tissue immunoprecipitated with PTMScan® Propionyl-Lysine [Prop-K] Immunoaffinity Beads. The logo represents the relative frequency of amino acids in each position surrounding the central propionylated lysine residue within this data set. | |
The chart shows the relative category distribution of proteins with propionylated lysine residues derived from peptides identified in a PTMScan® LC-MS/MS experiment of mouse liver tissue using PTMScan® Propionyl-Lysine Immunoaffinity Beads. |
