Reaction: acetyl-CoA + a [protein]-L-lysine = CoA + a [protein]-N6-acetyl-L-lysine
Other name(s): Nε-lysine acetyltransferase; KAT; peptidyl-lysine N-acetyltransferase; protein-N6-acetyl-L-lysine:CoA acetyltranferase; protein-lysine Nε-acetyltransferase
Systematic name: acetyl-CoA:[protein]-L-lysine N6-acetyltransferase
Comments: This entry stands for enzymes that catalyse the acetylation of the N6 of lysine residues within multiple proteins. Most enzymes are specific for a subset of proteins, though it could be very large. For example, YiaC from Escherichia coli targets 391 unique lysine residues in 251 proteins [3]. The reaction is reversible and in some cases the enzyme acts as deacetylase [4]. Some specific cases include EC 2.3.1.48, histone acetyltransferase, EC 2.3.1.108, α-tubulin N-acetyltransferase, and EC 2.3.1.309, [β-tubulin]-L-lysine N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Castano-Cerezo, S., Bernal, V., Rohrig, T., Termeer, S. and Canovas, M. Regulation of acetate metabolism in Escherichia coli BL21 by protein Nε-lysine acetylation. Appl. Microbiol. Biotechnol. 99 (2015) 3533-3545. [PMID: 25524697]
2. Zhang, Q., Zhou, A., Li, S., Ni, J., Tao, J., Lu, J., Wan, B., Li, S., Zhang, J., Zhao, S., Zhao, G.P., Shao, F. and Yao, Y.F. Reversible lysine acetylation is involved in DNA replication initiation by regulating activities of initiator DnaA in Escherichia coli. Sci. Rep. 6 (2016) 30837. [PMID: 27484197]
3. Christensen, D.G., Meyer, J.G., Baumgartner, J.T., D'Souza, A.K., Nelson, W.C., Payne, S.H., Kuhn, M.L., Schilling, B. and Wolfe, A.J. Identification of novel protein lysine acetyltransferases in Escherichia coli. mBio 9 (2018) e01905-18. [PMID: 30352934]
4. Rajendran, A., Vaidya, K., Mendoza, J., Bridwell-Rabb, J. and Kamat, S.S. Functional annotation of ABHD14B, an orphan serine hydrolase enzyme. Biochemistry 59 (2020) 183-196. [PMID: 31478652]