The Enzyme Database

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Accepted name: [histone H3]-lysine27 N-dimethyltransferase
Reaction: 2 S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-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
Other name(s): NSD3 (gene name)
Systematic name: S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-dimethyltransferase
Comments: This entry describes enzymes that successively methylate the L-lysine27 residue of histone H3 (H3K27) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins. The human NSD3 protein also catalyses the activity of EC, [histone H3]-lysine4 N-dimethyltransferase. cf. EC, [histone H3]-lysine27 N-methyltransferase, and EC, [histone H3]-lysine27 N-trimethyltransferase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
1.  Kim, S.M., Kee, H.J., Eom, G.H., Choe, N.W., Kim, J.Y., Kim, Y.S., Kim, S.K., Kook, H., Kook, H. and Seo, S.B. Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. Biochem. Biophys. Res. Commun. 345 (2006) 318–323. [PMID: 16682010]
[EC created 2020]

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