ENZYME entry: EC 18.104.22.168
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|[Histone-H3]-N(6),N(6)-dimethyl-L-lysine(4) FAD-dependent demethylase.
|Lysine-specific histone demethylase 1.|
|A [histone H3]-N(6),N(6)-dimethyl-L-lysine(4) + 2 acceptor + 2 H(2)O <=> a [histone H3]-L-lysine(4) + 2 formaldehyde + 2 reduced acceptor|
- The enzyme specifically removes methyl groups from mono- and
dimethylated lysine(4) of histone 3.
- During the reaction the substrate is oxidized by the FAD cofactor of
the enzyme to generate the corresponding imine, which is subsequently
hydrolyzed in the form of formaldehyde.The enzyme is similar to
flavin amine oxidases, and differs from all other known histone
lysine demethylases, which are iron(II)- and 2-oxoglutarate-dependent
- The physiological electron acceptor is not known with certainty.
- In vitro the enzyme can use oxygen, which is reduced to hydrogen
peroxide, but generation of hydrogen peroxide in the chromatin
environment is unlikely as it will result in oxidative damage of DNA.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
entries corresponding to 1.14.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-