Biology:Succinylation
From HandWiki
Succinylation is a posttranslational modification where a succinyl group (-CO-CH2-CH2-CO2H) is added to a cysteine residue of a protein molecule. This modification is found in many proteins, including histones.[1] The potential role of succinylation is under investigation, but as addition of succinyl group changes lysine's charge from +1 to −1 (at physiological pH) and introduces a relatively large structural moiety (100 Da), bigger than acetylation (42 Da) or methylation (14 Da), it is expected to lead to more significant changes in protein structure and function.[2]
By analogy to acetylation, it has been suggested that succinyl-CoA is the cofactor of enzyme-mediated lysine succinylation.
References
- ↑ Xie, Z.; Dai, J.; Dai, L.; Tan, M.; Cheng, Z.; Wu, Y.; Boeke, J. D.; Zhao, Y. (2012). "Lysine succinylation and lysine malonylation in histones". Molecular & Cellular Proteomics 11 (5): 100–7. doi:10.1074/mcp.M111.015875. PMID 22389435.
- ↑ Zhang, Z.; Tan, M.; Xie, Z.; Dai, L.; Chen, Y.; Zhao, Y. (2010). "Identification of lysine succinylation as a new post-translational modification". Nature Chemical Biology 7 (1): 58–63. doi:10.1038/nchembio.495. PMID 21151122.
External links
- Succinylation, Yet A Novel PTM Pathway for Biological Regulation, But Ready to Be Investigated
- Succinyl group at ChEBI
- The dawn of succinylation: a posttranslational modification.
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