Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy

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

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) R03875 R04866 R04867
Reaction

S-adenosyl-L-methionine [CPD:C00019];
[histone H3]-L-lysine27;
[histone H3]-N6-methyl-L-lysine27;
[histone H3]-N6,N6-dimethyl-L-lysine27

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.

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

1  [PMID:12351676]

2  [PMID:12435631]

3  [PMID:15231737]

4  [PMID:17200670]

5  [PMID:19026780]

6  [PMID:21317239]