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Information on EC 2.1.1.356 - [histone H3]-lysine27 N-trimethyltransferase

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IUBMB 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.
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
polycomb repressive complex 2, re-iibp, histone h3 lysine 27 methyltransferase, set domain histone lysine methyltransferase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = 3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
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overall reaction
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S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27
show the reaction diagram
(1a)
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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
show the reaction diagram
(1c)
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S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27
show the reaction diagram
(1b)
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PATHWAY SOURCE
PATHWAYS