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3 S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = 3 S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
overall reaction
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S-adenosyl-L-methionine + a [histone H4]-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6-methyl-L-lysine20
(1a)
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S-adenosyl-L-methionine + a [histone H4]-N6,N6-dimethyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6,N6-trimethyl-L-lysine20
(1c)
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S-adenosyl-L-methionine + a [histone H4]-N6-methyl-L-lysine20 = S-adenosyl-L-homocysteine + a [histone H4]-N6,N6-dimethyl-L-lysine20
(1b)
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S-adenosyl-L-methionine:[histone H4]-L-lysine20 N6-trimethyltransferase
The enzyme, characterized from the fission yeast Schizosaccharomyces pombe, catalyses three successive methylations of the L-lysine-20 residue of histone H4 (H4K20), forming the trimethylated form. The methylation of this site is apparently not involved in the regulation of gene expression or heterochromatin function but participates in DNA damage response. cf. EC 2.1.1.361, [histone H4]-lysine20 N-methyltransferase, and EC 2.1.1.362, [histone H4]-N-methyl-L-lysine20 N-methyltransferase.
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adenosyl-L-methionine + [histone H4]-N6,N6-dimethyl-L-lysine20
adenosyl-L-homocysteine + [histone H4]-N6,N6,N6-trimethyl-L-lysine20
S-adenosyl-L-methionine + [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-methionine + [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-homocysteine + [histone H4]-N6,N6-dimethyl-L-lysine20
additional information
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Substrates: enzyme shows versatility in substrate recognition. In a pan-methylation assay of histone H3, H3K4me3 and H3K27me3 species are preferably detected rather than me1 and me2 species, and H3K79-me1 and -me2 species are favored against me3 species. NSD3 shows significant di-/tri-methylation of histone H4K20
Products: -
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adenosyl-L-methionine + [histone H4]-N6,N6-dimethyl-L-lysine20
adenosyl-L-homocysteine + [histone H4]-N6,N6,N6-trimethyl-L-lysine20
Substrates: -
Products: -
?
adenosyl-L-methionine + [histone H4]-N6,N6-dimethyl-L-lysine20
adenosyl-L-homocysteine + [histone H4]-N6,N6,N6-trimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + [histone H4]-L-lysine20
S-adenosyl-L-homocysteine + [histone H4]-N6-methyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-homocysteine + [histone H4]-N6,N6-dimethyl-L-lysine20
Substrates: -
Products: -
?
S-adenosyl-L-methionine + [histone H4]-N6-methyl-L-lysine20
S-adenosyl-L-homocysteine + [histone H4]-N6,N6-dimethyl-L-lysine20
Substrates: -
Products: -
?
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Sanders, S.L.; Portoso, M.; Mata, J.; Bahler, J.; Allshire, R.C.; Kouzarides, T.
Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
Cell
119
603-614
2004
Schizosaccharomyces pombe (Q9USK2), Schizosaccharomyces pombe 972 (Q9USK2)
brenda
Morishita, M.; Mevius, D.; Di Luccio, E.
In vitro histone lysine methylation by NSD1, NSD2/MMSET/WHSC1 and NSD3/WHSC1L
BMC Struct. Biol.
14
25
2014
Homo sapiens (Q9BZ95)
brenda