Succinylation

{{short description|Addition of a succinyl group to a lysine group of a protein}}

In biochemistry, succinylation is a posttranslational modification where a succinyl group ({{chem2|\sCO\sCH2\sCH2\sCO2H}}) is added to a lysine residue of a protein molecule. This modification is found in many proteins, including histones.{{Cite journal

| last1 = Xie | first1 = Z.

| last2 = Dai | first2 = J.

| last3 = Dai | first3 = L.

| last4 = Tan | first4 = M.

| last5 = Cheng | first5 = Z.

| last6 = Wu | first6 = Y.

| last7 = Boeke | first7 = J. D.

| last8 = Zhao | first8 = Y.

| title = Lysine succinylation and lysine malonylation in histones

| doi = 10.1074/mcp.M111.015875

| journal = Molecular & Cellular Proteomics

| year = 2012

| pmid = 22389435

| pmc = 3418837| volume=11 | issue=5 | pages=100–7

| doi-access = free

}} 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.{{Cite journal

| last1 = Zhang | first1 = Z.

| last2 = Tan | first2 = M.

| last3 = Xie | first3 = Z.

| last4 = Dai | first4 = L.

| last5 = Chen | first5 = Y.

| last6 = Zhao | first6 = Y.

| doi = 10.1038/nchembio.495

| title = Identification of lysine succinylation as a new post-translational modification

| journal = Nature Chemical Biology

| volume = 7

| issue = 1

| pages = 58–63

| year = 2010

| pmid = 21151122

| pmc =3065206

}}

By analogy to acetylation, it has been suggested that succinyl-CoA is the cofactor of enzyme-mediated lysine succinylation.