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1.14.99.66: [histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase

This is an abbreviated version!
For detailed information about [histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase, go to the full flat file.

Word Map on EC 1.14.99.66

Reaction

a [histone H3]-N6,N6-dimethyl-L-lysine4
+ 2 acceptor + 2 H2O =
a [histone H3]-L-lysine4
+ 2 formaldehyde + 2 reduced acceptor

Synonyms

amine oxidase flavin-containing domain 1, amine-oxidase flavin-containing domain 1, AOF1, AOF2, BHC110, BHC110/LSD1, CG9088, demethylase LSD1, dJARID1/Lid, H3K4 demethylase, H3K4me2 demethylase, H3K4me2/1 histone demethylase, histone demethylase, histone H3 K4 demethylase, histone H3 lysine 4 demethylase, histone H3K4 demethylase, histone lysine-specific demethylase 1, Jarid1, KDM1, KDM1A, KDM1B, KIAA0601, LD40310, Lid, LSD1, LSD1 demethylase, LSD1/KDM1, LSD1/KDM1A, LSD2, lysine demethylase 1B, lysine specific demethylase 1, lysine-specific demethylase 1, lysine-specific demethylase 1A, lysine-specific demethylase 2, lysine-specific demethylase-1, lysine-specific histone demethylase, lysine-specific histone demethylase 1, lysine-specific histone demethylase 1A, lysine-specific histone demethylase 1B, lysinespecific demethylase 1, More, SPR-5

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase

Systematic Name

Systematic Name on EC 1.14.99.66 - [histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase

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SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6-dimethyl-L-lysine4:acceptor oxidoreductase (demethylating)
The enzyme specifically removes methyl groups from mono- and dimethylated lysine4 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 hydrolysed 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 dioxygenases. 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.