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1.14.11.68: [histone H3]-trimethyl-L-lysine27 demethylase

This is an abbreviated version!
For detailed information about [histone H3]-trimethyl-L-lysine27 demethylase, go to the full flat file.

Wordmap for 1.14.11.68

Word Map on EC 1.14.11.68 Wordmap for 1.14.11.68

Reaction

Show molfile
a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
+ 2 2-oxoglutarate + 2 O2 =
Show molfile
a [histone H3]-N6-methyl-L-lysine27
+ 2 succinate + 2 formaldehyde + 2 CO2

Synonyms

F18E9.5, histone demethylase, jmjd-3.1, JMJD3, KDM6A, Kdm6al, KDM6B, KDM6C, lysine-specific demethylase 6A, lysine-specific demethylase 6B, UTX, UTX1, UTY

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                EC 1.14.11.681.14.11.68 [histone H3]-trimethyl-L-lysine27 demethylase

Systematic Name

Systematic Name on EC 1.14.11.68 - [histone H3]-trimethyl-L-lysine27 demethylase

for references in articles please use BRENDA:EC1.14.11.68

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SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6,N6-trimethyl-L-lysine27,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 27 of histone H3 (H3K27). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri- and di-methylated forms, but have no activity with the mono-methylated form.