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a [histone H3]-N6,N6-dimethyl-L-lysine4 + ferricenium + H2O
a [histone H3]-N6-methyl-L-lysine4 + formaldehyde + ferrocene
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a [histone H3]-N6,N6-dimethyl-L-lysine4 + O2 + 2 H2O
a [histone H3]-L-lysine4 + 2 formaldehyde + 2 H2O2
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a [histone H3]-N6-methyl-L-lysine4 + acceptor + H2O
a [histone H3]-L-lysine4 + formaldehyde + reduced acceptor
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dimethylated histone 3-Lys4 peptide + H2O
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the enzyme specifically removes methyl groups from Lys4 of histone 3. The enzyme exhibits oxidase activity (with production of H2O2) but it can function also with a synthetic mono-electronic acceptor
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H3(1-20) K4-dimethylated peptide + 2-oxoglutarate + O2
H3(1-20) K4-monomethylated peptide + succinate + formaldehyde + CO2
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H3K4me2 (1-21 aa) peptide + 2-oxoglutarate + O2
H3K4me1 (1-21 aa) peptide + succinate + formaldehyde + CO2
H3K4me2 1-21 peptide + 2-oxoglutarate + O2
H3K4me1 1-21 peptide + succinate + formaldehyde + CO2
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H3K4me2 peptide 3-21 + 2-oxoglutarate + O2
H3K4me1 peptide 3-21 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
[histone H3 peptide 21mer P16A]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
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[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3 peptide 21mer]-N6,N6-dimethyl-L-lysine4-dimethyl-L-lysine9 + 2-oxoglutarate + O2
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[histone H3 peptide 21mer]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4 + succinate + formaldehyde + CO2
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no activity with a monomethylated H3-Lys4 peptide with Arg2 mutated to Ala, Arg2 is central to substrate recognition also in LSD2
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[histone H3 peptide 21mer]-N6-methyl-L-lysine4-acetyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3 peptide 21mer]-L-lysine4-acetyl-L-lysine9 + succinate + formaldehyde + CO2
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[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-arginine17 + 2-oxoglutarate + O2
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[histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-lysine9 + 2-oxoglutarate + O2
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[histone H3 peptide 30mer]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide 30mer]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + acceptor + H2O
[histone H3]-N6-methyl-L-lysine 4 + formaldehyde + reduced acceptor
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[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 acceptor + 2 H2O
[histone H3]-L-lysine4 + 2 formaldehyde + 2 reduced acceptor
overall reaction
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[histone H3]-N6,N6-L-dimethyllysine21 + O2 + 2 H2O
[histone H3]-L-lysine + 2 formaldehyde + 2 H2O2
diMeK4H3-21 i.e. a dimethyl K4-containing histone H3 peptide
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[histone H3]-N6,N6-L-dimethyllysine4 + O2 + 2 H2O
[histone H3]-N6,N6-L-dimethyllysine4 + 2 formaldehyde + 2 H2O2
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[histone H3]-N6,N6-L-dimethyllysine4-1-21 + O2 + 2 H2O
[histone H3]-L-lysine4-1-21 + 2 formaldehyde + 2 H2O2
substrate is a dimethylated peptide corresponding to the first 21 amino acids of the N-terminal tail of histone H3
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[histone H3]-N6,N6-methyl-L-lysine 4 + acceptor + H2O
[histone H3]-L-lysine 4 + formaldehyde + reduced acceptor
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone H4]-N6-methyl-L-lysine 20 + 2-oxoglutarate + O2
[histone H4]-L-lysine 20 + succinate + formaldehyde + CO2
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additional information
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H3K4me2 (1-21 aa) peptide + 2-oxoglutarate + O2
H3K4me1 (1-21 aa) peptide + succinate + formaldehyde + CO2
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H3K4me2 (1-21 aa) peptide + 2-oxoglutarate + O2
H3K4me1 (1-21 aa) peptide + succinate + formaldehyde + CO2
a peptide corresponding to the first 21 amino acids of histone H3 with a dimethylated lysine at the fourth residue [ARTK(diMe)QTARKSTGGKAPRKQLA]
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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dimethyl-H3K4 is an activation markers for gene expression
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
dimethyl-H3K4 is an activation markers for gene expression
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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lack of H3K4diMe is possibly due to complex epigenetic regulation involving Ash2 and LSD1
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
specific pockets in the substrate-binding site of LSD1 that interact with several H3 side chains, Thr6, Arg8, Lys9 and Thr11, and also with the N-terminal amino group of Ala1, N-term pocket, overview
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
specific pockets in the substrate-binding site of LSD1 that interact with several H3 side chains, Thr6, Arg8, Lys9 and Thr11, and also with the N-terminal amino group of Ala1, N-term pocket
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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additional information
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LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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additional information
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LSD1 shows demethylase activity toward mono- and dimethylated Lys4 but not dimethylated Lys9 and Lys27 of histone 3, substrate and product identification by MALDI mass spectrometry. No LSD1 activity toward the H3K4me1-phosphoSer10 peptide
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additional information
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LSD1 shows demethylase activity toward mono- and dimethylated Lys4 but not dimethylated Lys9 and Lys27 of histone 3, substrate and product identification by MALDI mass spectrometry. No LSD1 activity toward the H3K4me1-phosphoSer10 peptide
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additional information
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LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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additional information
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LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview
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additional information
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LSD1 catalyzes the demethylation of Lys4 of histone H3 through a flavin-dependent oxidative reaction via an imine intermediate. LSD1 can act both on mono- and dimethylated H3K4. The reaction involves several steps, overview
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additional information
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LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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additional information
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the fly KDM1 protein has in vitro demethylase activity for H3K4me2/1
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additional information
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functional interplay between histone demethylase and histone deacetylase
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additional information
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LSD1 forms a complex with CoREST and histone deacetylase 1. LSD1 mediates the transrepressive function of TLX, an orphan nuclear receptor, also called NR2E1, that regulates the expression of target genes by functioning as a constitutive transrepressor, through direct interaction via its SWIRM and amine oxidase domains. Physiological significance of TLX in the cytodifferentiation of neural cells in the brain
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additional information
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LSD1 forms a stable complex with Rb, but with E2F1, cell cycle regulatory proteins. LSD1 binds to Epstein-Barr virus C promoter Cp in a cell cycle-dependent manner, as do the the cell cycle regulatory proteins E2F1 and Rb. Rb and LSD1 binding to Cp increase after the S phase, corresponding to a decrease in histone H3 K4 methylation and Cp transcription, overview
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additional information
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LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes
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additional information
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LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview. LSD1 forms a complex with CoREST, structure with bound histone H3 peptide substrate, overview. LSD1 tightly associates with the CoREST C-terminal SANT domain. This intermolecular association is mediated by the LSD1 tower domain, whose alpha-helices are embraced by a helical segment of CoREST, generating an intermolecular helical coil. The histone H3 N-terminal peptide binds deeply in the LSD1 amine oxidase domain in proximity to the flavin cofactor
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additional information
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LSD1 catalyzes the demethylation of Lys4 of histone H3 through a flavin-dependent oxidative reaction via an imine intermediate. LSD1 can act both on mono- and dimethylated H3K4. The reaction involves several steps, overview
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additional information
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LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview
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additional information
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LSD1 specificity and mechanism of action are complex-dependent
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additional information
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LSD1 removes the methyl groups from lysines 4 and 9 of histone 3 with the generation of formaldehyde from the methyl group
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additional information
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LSD1 directly binds to the promoter of P21 where it catalyzes H3K4me2 demethylation. FEZF1-AS1, a 2564 bp RNA overexpressed in gastric cancer, epigenetically represses the expression of P21 via binding with LSD1
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additional information
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lysine-specific demethylase 1(LSD1) demethylates mono- and dimethylated residues of lysine-4 on histone H3 (H3K4me1 and H3K4me2) and lysine-9 on histone H3 (H3K9me1 and H3K9me2)
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additional information
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histone demethylase LSD1 demethylates Lys4 or Lys9 of histone H3 using FAD as cofactor
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additional information
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no substrates: dimethylated histone H3 K9 residues
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65)
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65)
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65), as well as non-histone substrates. Tight-binding nature of the H3/KDM1A interaction, kinetics, overview. No other core histones exhibits inhibition of KDM1A demethylation activity, which is consistent with H3 being the preferred histone substrate of KDM1A versus H2A, H2B, and H4. Kinetic analysis of full-length histone products against KDM1A. KDM1A requires a minimal substrate corresponding to the first 21 residues of the N-terminal histone H3 tail for efficient demethylation activity. Recombinant KDM1A/LSD11 forms a complex in vitro with recombinant transcription factor CoREST
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65). Functional interplay between histone demethylase and histone deacetylase. The enzymatic activities of the histone demethylase and the deacetylase are intimately linked. The cross talk between the two enzymes is seen only when nucleosomal substrates are used and is mediated through different domains of the CoREST protein (FLAG-tagged CoREST and mutants are recombinantly expressed in HEK-293 cells and Escherichia coli strain BL21). LSD1-HDAC1 complexes display enhanced acetylation activity in presence of CoREST
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65). LSD1 is specific for Lys-4 of histone H3 and can oxidatively demethylate the dimethyl or monomethyl Lys-containing substrates
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1. As LSD1 can demethylate both H3K4 and H3K9, the coupling of this protein in the HCF-1 Set1 or MLL methyltransferase complex may enhance H3K9 demethylation or preferentially target it to this substrate, although additional histone modifications and modification activities may also contribute to the H3K4 or H3K9 recognition and specificity
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the enzyme is specific for mono- and dimethylated Lys4 in histone H3 (H3K4me1/2). LSD1 prefers an unmodified alpha-amine three residues preceding the methyllysine in the protein substrate, consistent with its specificity for H3K4me1/2 in vitro. To catalyze efficient demethylation, the enzyme requires H3 peptides at least 16 residues in length. In addition, LSD1 exhibits a strong preference toward H3K4me2 substrates lacking other covalent modifications, including R2me, R8me, S10ph, K9ac, and K14ac. In addition, LSD1 might also by active with mono- and dimethylated Lys9 in histone H3 (H3K9me1/2), cf. EC 3.4.11.66
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the rate-limiting reductive half-reaction of LSD1 employs a direct hydride transfer mechanism. Conserved residue Tyr761 and the lysine-water-flavin motif help properly orienting FAD with respect to substrate, thereby stabilizing the catalytic environment and facilitating the demethylation reaction
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amine oxidase flavin-containing domain 1, AOF1, also called lysine demethylase 1B , KDM1B, is a protein related to the lysine demethylase KDM1or LSD1, it functions as a H3K4 demethylase and is required for de novo DNA methylation of some imprinted genes in oocytes
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p53 directly interacts with LSD1 to alter chromatin structure and confer developmental repression of the tumor marker alpha-fetoprotein, AFP, p53 and LSD1 cooccupy a p53 response element, concomitant with dimethylated histone H3 lysine 4 demethylation and postnatal repression of AFP transcription, overview
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the enzyme is organized in histone demethylase complexes containing LSD1, RE1 silencing transcription factor corepressor, CoREST, histone deacetylase 1, HDAC1, and histone deacetylase 2 in erythroleukemia and T cell leukemia cells. the Complex interacts with TAL, a critical transcription factor required for hematopoiesis, overview. The enzymatic domain of LSD1 plays an important role in repressing the TAL1-directed transcription, overview. TAL1-associated LSD1 and HDM activity are dynamically regulated during hematopoiesis
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recombinant KDM1B shows no activity with H3K4me3, H3K9me2, H3K27me2 and H3K36me2
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substrate specificity and effect of epigenetic marks, overview. No activity with peptide substrate of chain length below 21. Activity determinations of recombinant wild-type and mutant enzymes by horseradish peroxidase-coupled and formaldehyde dehydrogenase-coupled assays with histone H3 peptides as substrates, method optimization, e.g. with respect to pH and ionic strength, overview
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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no activity with histone H3 N6,N6,N6-dimethyl-L-lysine4
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no activity with histone H3 N6,N6,N6-dimethyl-L-lysine4
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the bifunctional enzyme catalyzes the demethylation of H3K4me2/me1 and H3K9me2/me1 (EC 1.14.11.65)
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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additional information
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the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1
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