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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.

Word Map on EC 1.14.11.68

Reaction

a [histone H3]-N6,N6,N6-trimethyl-L-lysine27
+ 2 2-oxoglutarate + 2 O2 =
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
                1.14.11.68 [histone H3]-trimethyl-L-lysine27 demethylase

Crystallization

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

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the catalytic fragment of UTX/KDM6A, in the free and H3 peptide-bound forms. The catalytic jumonji domain binds H3 residues 25-33, recognizing H3R26, H3A29, and H3P30 in a sequence-specific manner, in addition to H3K27me3 in the catalytic pocket. A zinc-binding domain, conserved within the KDM6 family, binds residues 17-21 of H3. The zinc-binding domain changes its conformation upon H3 binding, and thereby recognizes the H3L20 side chain via a hydrophobic patch on its surface, which is inaccessible in the H3-free form. Residues H3R17, H3L20, H3R26, H3A29, H3P30, and H3T32 are each important for demethylation