[histone-H3]-lysine-36 demethylase;
JHDM1A;
JmjC domain-containing histone demethylase 1A;
H3-K36-specific demethylase;
histone-lysine (H3-K36) demethylase;
histone demethylase;
protein-6-N,6-N-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase

Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

protein-N6,N6-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase

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

R09510 R09511 R10056

protein N6,N6-dimethyl-L-lysine [CPD:C05545];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007];
protein N6-methyl-L-lysine [CPD:C05544]

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 Lys-36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. It can also demethylate the monomethyl- but not the trimethyl form of Lys-36.

1  [PMID:16362057]

Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y.

Histone demethylation by a family of JmjC domain-containing proteins.

Nature. 439 (2006) 811-6.

Homo sapiens [GN:hsa], Saccharomyces cerevisiae [GN:sce]