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EC 1.14.99.66 Details
show Brenda entryEC number
1.14.99.66
Accepted name
[histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase
Reaction
a [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 acceptor + 2 H2O = a [histone H3]-L-lysine4 + 2 formaldehyde + 2 reduced acceptor (overall reaction);;(1a) a [histone H3]-N6,N6-dimethyl-L-lysine4 + acceptor + H2O = a [histone H3]-N6-methyl-L-lysine4 + formaldehyde + reduced acceptor;;(1b) a [histone H3]-N6-methyl-L-lysine4 + acceptor + H2O = a [histone H3]-L-lysine4 + formaldehyde + reduced acceptor
Other name(s)
KDM1 (gene name),
LSD1 (gene name),
lysine-specific histone demethylase 1
Systematic name
[histone H3]-N6,N6-dimethyl-L-lysine4:acceptor oxidoreductase (demethylating)
Comment
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.
History
created 2019
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000 1.14.99.6 created 1972, modified 2000, deleted 2000 1.14.99.8 created 1972, deleted 1984 1.14.99.13 created 1972, deleted 1984 1.14.99.16 created 1972, deleted 2002 1.14.99.17 created 1972, deleted 1976 1.14.99.18 created 1976, modified 1999, deleted 2003 1.14.99.25 created 1986, deleted 2000
