The Enzyme Database

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EC 1.14.11.27     
Accepted name: [histone H3]-dimethyl-L-lysine36 demethylase
Reaction: 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)
(1a) a [histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
(1b) a [histone H3]-N6-methyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-L-lysine36 + succinate + formaldehyde + CO2
Other name(s): KDM2A (gene name); KDM2B (gene name); JHDM1A (gene name); JHDM1B (gene name); JmjC domain-containing histone demethylase 1A; H3-K36-specific demethylase (ambiguous); histone-lysine (H3-K36) demethylase (ambiguous); histone demethylase (ambiguous); protein-6-N,6-N-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase; protein-N6,N6-dimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase; [histone-H3]-lysine-36 demethylase
Systematic name: [histone H3]-N6,N6-dimethyl-L-lysine36,2-oxoglutarate:oxygen oxidoreductase
Comments: 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Tsukada, Y., Fang, J., Erdjument-Bromage, H., Warren, M.E., Borchers, C.H., Tempst, P. and Zhang, Y. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439 (2006) 811–816. [DOI] [PMID: 16362057]
[EC 1.14.11.27 created 2006, modified 2019]
 
 


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