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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

Crystallization

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

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination of LSD1/CoREST complex bound to histone H3 peptides, and of LSD1 complexed with a suicide inhibitor consisting of a 21-residue histone H3 peptide in which K4 is modified by an N-methylpropargyl group
enzyme complex LSD1-CoREST crystal structure in complex with a histone H3 peptide, overview
-
in complex with inhibitor tranylcypromine, diffraction to 2.25 A. In the inhibitor-free structure, a water molecule forms a hydrogen bond with the flavin N(5) atom and Lys661. The LSD1-tranylcypromine complex is not completely composed of the five-membered adduct, but partially contains an intermediate
modeling of the complex composed of LSD1, cofactor CoREST, and histone substrate
molecular docking of inhibitor 3-[(E)-2-[2-(5-fluoro-2-hydroxyphenyl)pyridin-4-yl]ethenyl]N'-hydroxybenzene-1-carboximidamide. Compound can be well docked into the FAD binding site of LSD1
molecular docking of inhibitors
purified recombinant truncated enzyme LSD1 comprising residues 172-833 in complex with recombinant human CoREST residues 308-440, and peptide inhibitors 9, 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/m 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 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, 11 or 13 for 2 h, X-ray diffraction structure determination and analysis at 2.53-2.69 A resolution
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 enzyme, hanging-drop vapor diffusion method, 2.8 A-resolution crystal structure
-
recombinant GST-tagged enzyme fragment in complex with inhibitor tranylcypromine, X-ray diffraction structure determination and analysis at 2.25 A resolution
structure of LSD1 in complex with cofactor CoREST and inhibitor rans-2-phenylcyclopropylamine. The inhibitor forms a covalent adduct with FAD in LSD1. The phenyl ring of the FAD-inhibitor adduct does not form extensive interactions with active-site residues