ExplorEnz: EC 2.3.1.338

Your query returned 1 entry. Printable version

2.3.1.338

Accepted name:

[protein]-L-lysine N-acetyltransferase

Reaction:

acetyl-CoA + a [protein]-L-lysine = CoA + a [protein]-N⁶-acetyl-L-lysine

Other name(s):

N^ε-lysine acetyltransferase; KAT; peptidyl-lysine N-acetyltransferase; protein-N⁶-acetyl-L-lysine:CoA acetyltranferase; protein-lysine N^ε-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

References:

1.	Castano-Cerezo, S., Bernal, V., Rohrig, T., Termeer, S. and Canovas, M. Regulation of acetate metabolism in Escherichia coli BL21 by protein N^ε-lysine acetylation. Appl. Microbiol. Biotechnol. 99 (2015) 3533–3545. [DOI] [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. 6:30837 (2016). [DOI] [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:e01905-18 (2018). [DOI] [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. [DOI] [PMID: 31478652]

[EC 2.3.1.338 created 2026]