ExplorEnz: EC 2.1.1.356

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2.1.1.356

Accepted name:

[histone H3]-lysine²⁷ N-trimethyltransferase

Reaction:

3 S-adenosyl-L-methionine + a [histone H3]-L-lysine²⁷ = 3 S-adenosyl-L-homocysteine + a [histone H3]-N⁶,N⁶,N⁶-trimethyl-L-lysine²⁷ (overall reaction)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine²⁷ = S-adenosyl-L-homocysteine + a [histone H3]-N⁶-methyl-L-lysine²⁷
(1b) S-adenosyl-L-methionine + a [histone H3]-N⁶-methyl-L-lysine²⁷ = S-adenosyl-L-homocysteine + a [histone H3]-N⁶,N⁶-dimethyl-L-lysine²⁷
(1c) S-adenosyl-L-methionine + a [histone H3]-N⁶,N⁶-dimethyl-L-lysine²⁷ = S-adenosyl-L-homocysteine + a [histone H3]-N⁶,N⁶,N⁶-trimethyl-L-lysine²⁷

Other name(s):

KMT6A (gene name); KMT6B (gene name); EZH1 (gene name); EZH₂ (gene name)

Systematic name:

S-adenosyl-L-methionine:[histone H3]-L-lysine²⁷ N⁶-trimethyltransferase

Comments:

This entry describes enzymes that successively methylate the L-lysine²⁷ residue of histone H3 (H3K27), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. The methylation of lysine²⁷ leads to transcriptional repression of the affected target genes. The enzyme associates with other proteins to form a complex that is essential for activity. The enzyme can also methylate some non-histone proteins. cf. EC 2.1.1.369, [histone H3]-lysine²⁷ N-methyltransferase and EC 2.1.1.371, [histone H3]-lysine²⁷ N-dimethyltransferase.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R.S. and Zhang, Y. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298 (2002) 1039–1043. [PMID: 12351676]
2.	Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P. and Reinberg, D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16 (2002) 2893–2905. [PMID: 12435631]
3.	Kirmizis, A., Bartley, S.M., Kuzmichev, A., Margueron, R., Reinberg, D., Green, R. and Farnham, P.J. Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27. Genes Dev. 18 (2004) 1592–1605. [PMID: 15231737]
4.	Schlesinger, Y., Straussman, R., Keshet, I., Farkash, S., Hecht, M., Zimmerman, J., Eden, E., Yakhini, Z., Ben-Shushan, E., Reubinoff, B.E., Bergman, Y., Simon, I. and Cedar, H. Polycomb-mediated methylation on Lys²⁷ of histone H3 pre-marks genes for de novo methylation in cancer. Nat. Genet. 39 (2007) 232–236. [PMID: 17200670]
5.	Shen, X., Liu, Y., Hsu, Y.J., Fujiwara, Y., Kim, J., Mao, X., Yuan, G.C. and Orkin, S.H. EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol. Cell 32 (2008) 491–502. [PMID: 19026780]
6.	Ezhkova, E., Lien, W.H., Stokes, N., Pasolli, H.A., Silva, J.M. and Fuchs, E. EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair. Genes Dev. 25 (2011) 485–498. [PMID: 21317239]

[EC 2.1.1.356 created 1976 as EC 2.1.1.43, modified 1982, modified 1983, part transferred 2019 to EC 2.1.1.356, modified 2020]