Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy

[histone H3]-N6,N6-dimethyl-L-lysine36,2-oxoglutarate:oxygen oxidoreductase

a [histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2 (overall reaction) [RN:R10056];
(1a) a [histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2 [RN:R09510];
(1b) a [histone H3]-N6-methyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-L-lysine36 + succinate + formaldehyde + CO2 [RN:R09511]

R09510 R09511 R10056
Reaction

[histone H3]-N6,N6-dimethyl-L-lysine36;
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007];
[histone H3]-N6-methyl-L-lysine36

Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys36 (K36me2), which is its natural substrate, to form the monomethylated and unmethylated forms of Lys36. It can also demethylate monomethylated (but not the trimethylated) Lys36. cf. EC 1.14.11.69, [histone H3]-trimethyl-L-lysine36 demethylase.

EC 1.14.11.27 created 2006, modified 2019

1  [PMID:16362057]