Succinylation of proteins on the epsilon-amino group of lysine residues is a posttranslational modification that is still poorly understood.
Epsilon-succinyl lysine is known as a target of certain Sirtuins, a class of enzymes that has attracted attention for their role in metabolic regulation, disease pathogenesis and ageing. Synthetic succinyl lysine may aid in the understanding of the role of lysine succinylation, as well as in the further elucidation of Sirtuin function.
Succinyl modifications on proteins are removed by certain Sirtuins (R1, R2 = peptide chain).
→ Lysines with different epsilon-acyl groups are available via our Custom Synthesis service.
- Site-Specific Installation of Succinyl Lysine Analog into Histones Reveals the Effect of H2BK34 Succinylation on Nucleosome Dynamics; Y. Jing, Z. Liu, G. Tian, X. Bao, T. Ishibashi and X. D. Li; Cell Chemical Biology 2018; 25: 166-174.e7. doi:https://doi.org/10.1016/j.chembiol.2017.11.005
- The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications; C. Carrico, J. G. Meyer, W. He, B. W. Gibson and E. Verdin; Cell Metabolism 2018; 27: 497-512. doi:https://doi.org/10.1016/j.cmet.2018.01.016
- A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation; G. R. Wagner, D. P. Bhatt, T. M. O’Connell, J. W. Thompson, L. G. Dubois, D. S. Backos, H. Yang, G. A. Mitchell, O. R. Ilkayeva, R. D. Stevens, P. A. Grimsrud and M. D. Hirschey; Cell Metabolism 2017; 25: 823-837.e8. doi:https://doi.org/10.1016/j.cmet.2017.03.006
- SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion; K. A. Anderson, F. K. Huynh, K. Fisher-Wellman, J. D. Stuart, B. S. Peterson, J. D. Douros, G. R. Wagner, J. W. Thompson, A. S. Madsen, M. F. Green, R. M. Sivley, O. R. Ilkayeva, R. D. Stevens, D. S. Backos, J. A. Capra, C. A. Olsen, J. E. Campbell, D. M. Muoio, P. A. Grimsrud and M. D. Hirschey; Cell Metabolism 2017; 25: 838-855.e15. doi:https://doi.org/10.1016/j.cmet.2017.03.003
- Lysine Succinylation Is a Frequently Occurring Modification in Prokaryotes and Eukaryotes and Extensively Overlaps with Acetylation; Brian T. Weinert, C. Schölz, Sebastian A. Wagner, V. Iesmantavicius, D. Su, Jeremy A. Daniel and C. Choudhary; Cell Reports 2013; 4: 842-851. doi:https://doi.org/10.1016/j.celrep.2013.07.024
- SIRT5 Regulates the Mitochondrial Lysine Succinylome and Metabolic Networks; Matthew J. Rardin, W. He, Y. Nishida, John C. Newman, C. Carrico, Steven R. Danielson, A. Guo, P. Gut, Alexandria K. Sahu, B. Li, R. Uppala, M. Fitch, T. Riiff, L. Zhu, J. Zhou, D. Mulhern, Robert D. Stevens, Olga R. Ilkayeva, Christopher B. Newgard, Matthew P. Jacobson, M. Hellerstein, Eric S. Goetzman, Bradford W. Gibson and E. Verdin; Cell Metabolism 2013; 18: 920-933. doi:https://doi.org/10.1016/j.cmet.2013.11.013
- SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways; J. Park, Y. Chen, Daniel X. Tishkoff, C. Peng, M. Tan, L. Dai, Z. Xie, Y. Zhang, Bernadette M. M. Zwaans, Mary E. Skinner, David B. Lombard and Y. Zhao; Molecular Cell 2013; 50: 919-930. doi:https://doi.org/10.1016/j.molcel.2013.06.001
- Sirtuin mechanism and inhibition: explored with Nε-acetyl-lysine analogs; B. M. Hirsch and W. Zheng; Molecular BioSystems 2011; 7: 16-28. doi:10.1039/c0mb00033g