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1.14.11.65: [histone H3]-dimethyl-L-lysine9 demethylase

This is an abbreviated version!
For detailed information about [histone H3]-dimethyl-L-lysine9 demethylase, go to the full flat file.

Word Map on EC 1.14.11.65

Reaction

a [histone H3]-N6,N6-dimethyl-L-lysine9
+ 2 2-oxoglutarate + 2 O2 =
a [histone H3]-L-lysine9
 + 2 succinate + 2 formaldehyde + 2 CO2

Synonyms

AOF2, AtJMJ17, BHC110, G9A/KMT1C, GLP/KMT1D, H3K4me2 demethylase, H3K9 demethylase, H3K9 histone demethylase, H3K9 Jumonji demethylase, H3K9 mono- and di-demethylase, H3K9Me2 demethylase, H3K9me2 methylase, H3K9me3 methylase, hairless, hairless protein, HDM, histone demethylase, histone demethylase JMJD1C, histone H3 Lys 9 demethylase, histone H3 lysine 9 demethylase, histone H3 lysine 9 Jumonji demethylase, histone H3 lysine 9 mono- and di-demethylase, histone H3K9 demethylase, histone lysine demethylase, IBM1, JHDM2A, JMJ25, JMJ27, JmjC domain-containing protein 27, jmjC histone demethylase, JmjC-domain-containing histone demethylase 2A, JMJD1A, JMJD1B, JMJD2A, Jmjd2c histone demethylase, KDM1, KDM1A, Kdm3a, Kdm3b, KDM4A, KDM7A, KIAA0601, KIAA1718, LSD1, LSD1 demethylase, LSD1/KDM1, LSD2, lysine specific demethylase 1, lysine-specific demethylase 1, lysine-specific demethylase 1A, lysine-specific demethylase 3A, lysine-specific demethylase-1, lysine-specific histone demethylase 1, lysine-specific histone demethylase 2, More, NPAO, p110b, PHF8, PHF8/KIAA1718 histone demethylase, plant homeodomain finger protein 8, SPAC23E2.02, SPBC146.09c, Suv(Var)3-9/KMT1, SWIRM1, SWIRM2, Swm1, Swm1/2 complex, Swm2, [histone-H3]-lysine-4-demethylase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.65 [histone H3]-dimethyl-L-lysine9 demethylase

Crystallization

Crystallization on EC 1.14.11.65 - [histone H3]-dimethyl-L-lysine9 demethylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor E67
purified recombinant truncated enzyme LSD1 comprising residues 172-833 in complex with recombinant human CoREST residues 308-440, and peptide inhibitors L-seryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucine, N2-L-seryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-(N6-(L-seryl))-L-lysine-amide, and L-homoseryseryl-L-arginyl-L-threonyl-L-methionyl-L-glutaminyl-L-threonyl-L-alanyl-L-arginyl-L-lysyl-L-seryl-L-threonylglycylglycyl-L-lysyl-L-alanyl-L-prolyl-L-arginyl-L-lysyl-L-glutaminyl-L-leucyl-(N6-(L-homoseryl))-L-lysine, by hanging drop vapor diffusion method, mixing of 0.001 ml of 9 mg/ml protein solution with 0.001 ml of reservoir solution containing 100 mM N-(carbamoylmethyl)iminodiacetic acid, pH 5.5, and 1.18-1.28M potassium sodium tartrate tetrahydrate, 20°C, crystals are soaked in a solution containing 100 mM N-(carbamoylmethyl) iminodiacetic acid buffer, pH 5.5, with 1.14 M potassium sodium tartrate tetrahydrate, 10% glycerol, and 2 mM LSD1 inhibitor peptide for 2 h, X-ray diffraction structure determination and analysis at 2.53-2.69 A resolution
recombinant GST-tagged enzyme fragment in complex with inhibitor tranylcypromine, X-ray diffraction structure determination and analysis at 2.25 A resolution