MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsComposite Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: [histone-H3]-lysine-36 demethylase

Enzyme Commission Synonyms: 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

Taxonomic Range: Metazoa, Fungi

a [protein] N6,N6-dimethyl-L-lysine + 2-oxoglutarate + oxygen → a [protein] N6-methyl-L-lysine + succinate + formaldehyde + CO2,
a [protein] N6-methyl-L-lysine + 2-oxoglutarate + oxygen + H+ → a [protein]-L-lysine + succinate + formaldehyde + CO2

Standard Gibbs Free Energy (ΔrG in kcal/mol): -164.16656Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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.

Citations: [Tsukada06]

Unification Links: KEGG:R10056

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:

Created 15-Mar-2012 by Caspi R, SRI International


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Tsukada06: Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y (2006). "Histone demethylation by a family of JmjC domain-containing proteins." Nature 439(7078);811-6. PMID: 16362057

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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