Succinylation
Jump to navigation
Jump to search
In biochemistry, succinylation is a posttranslational modification where a succinyl group (−CO−CH2−CH2−CO2H) is added to a lysine 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.