PTMScan® Glutaryl-Lysine [Glut-K] Kit #26101
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Background
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).
Lysine glutarylation events predominate in the mitochondria and mainly occur on metabolic proteins. Similar to malonylation and succinylation, lysine glutaryl transfer is likely mediated by a combination of non-enzymatic, thermodynamic, and stoichiometric mechanisms driving the reaction in the acidic environment of the mitochondria in the presence of promiscuous acetyltransferases (6). SirT5 and glutaryl-CoA dehydrogenase (GCDH) knockout mice exhibit elevated levels of glutarylated proteins as do mice on a diet high in tryptophan. SirT5 is likely the main de-glutarylase, as demonstrated by its activity on carbamoyl phosphate synthase 1 (CPS1), a heavily glutarylated protein of the urea cycle (7).
- 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.
- Hirschey, M.D. and Zhao, Y. (2015) Mol Cell Proteomics [Epub ahead of print]
- Tan, M. et al. (2014) Cell Metab 19, 605-17.
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