| EC |
2.1.1.369 |
| Accepted name: |
[histone H3]-lysine27 N-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27 |
| Other name(s): |
ATXR5 (gene name) |
| Systematic name: |
S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase |
| Comments: |
This entry describes enzymes that methylate the L-lysine-27 residue of histone H3 only once, generating a monomethylated form. This modification influences the binding of chromatin-associated proteins. The methylation of lysine-27 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.371, [histone H3]-lysine27 N-dimethyltransferase, and EC 2.1.1.356, [histone H3]-lysine27 N-trimethyltransferase. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Jacob, Y., Feng, S., LeBlanc, C.A., Bernatavichute, Y.V., Stroud, H., Cokus, S., Johnson, L.M., Pellegrini, M., Jacobsen, S.E. and Michaels, S.D. ATXR5 and ATXR6 are H3K27 monomethyltransferases required for chromatin structure and gene silencing. Nat. Struct. Mol. Biol. 16 (2009) 763–768. [PMID: 19503079] |
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| [EC 2.1.1.369 created 2020] |
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