The Enzyme Database

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Accepted name: [histone H3]-lysine4 N-methyltransferase
Reaction: S-adenosyl-L-methionine + a [histone H3]-L-lysine4 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine4
Other name(s): KMT7 (gene name); SETD7 (gene name); SET7/9 (gene name); KIAA1717 (gene name); KMT2A (gene name); KMT2B (gene name); KMT2C (gene name); KMT2D (gene name); KMT2F (gene name); KMT2G (gene name); MLL1 (gene name); MLL2 (gene name); MLL3 (gene name); MLL4 (gene name); SETD1A (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-methyltransferase
Comments: This entry describes enzymes that catalyse a single methylation of the L-lysine4 residue of histone H3 (H3K4), generating a monomethylated form. This modifications influence the binding of chromatin-associated proteins and result in gene activation or suppression. Some enzymes that catalyse this reaction continue to generate a dimethyated form, these enzymes are classified under EC, [histone H3]-lysine4 N-dimethyltransferase. Other enzymes continue to catalyse a third methylation, those are classified under EC, [histone H3]-lysine4 N-trimethyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Wang, H., Cao, R., Xia, L., Erdjument-Bromage, H., Borchers, C., Tempst, P. and Zhang, Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8 (2001) 1207–1217. [PMID: 11779497]
2.  Nishioka, K., Chuikov, S., Sarma, K., Erdjument-Bromage, H., Allis, C.D., Tempst, P. and Reinberg, D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16 (2002) 479–489. [PMID: 11850410]
3.  Wilson, J.R., Jing, C., Walker, P.A., Martin, S.R., Howell, S.A., Blackburn, G.M., Gamblin, S.J. and Xiao, B. Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell 111 (2002) 105–115. [PMID: 12372304]
4.  Xiao, B., Jing, C., Wilson, J.R., Walker, P.A., Vasisht, N., Kelly, G., Howell, S., Taylor, I.A., Blackburn, G.M. and Gamblin, S.J. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421 (2003) 652–656. [PMID: 12540855]
5.  Hu, P. and Zhang, Y. Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures. J. Am. Chem. Soc. 128 (2006) 1272–1278. [PMID: 16433545]
6.  Patel, A., Dharmarajan, V., Vought, V.E. and Cosgrove, M.S. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J. Biol. Chem. 284 (2009) 24242–24256. [DOI] [PMID: 19556245]
7.  Shinsky, S.A., Monteith, K.E., Viggiano, S. and Cosgrove, M.S. Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation. J. Biol. Chem. 290 (2015) 6361–6375. [DOI] [PMID: 25561738]
[EC created 1976 as EC, modified 1982, modified 1983, part transferred 2020 to EC]

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